Diversity of the lysozyme fold: structure of the catalytic domain from an unusual endolysin encoded by phage Enc34

Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The cataly...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports Vol. 12; no. 1; pp. 5005 - 11
Main Authors: Cernooka, Elina, Rumnieks, Janis, Zrelovs, Nikita, Tars, Kaspars, Kazaks, Andris
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 23.03.2022
Nature Publishing Group
Nature Portfolio
Subjects:
631/337
631/535
Bacteria
Bacterial diseases
Bacteriophages - metabolism
Catalytic Domain
Conserved sequence
Crystal structure
Endopeptidases - metabolism
Enzymes
Glycoside hydrolase
Gram-negative bacteria
Humanities and Social Sciences
Lysozyme
multidisciplinary
Multidrug resistance
Muramidase - metabolism
Opportunist infection
Peptidoglycan - metabolism
Peptidoglycans
Phages
Science
Science (multidisciplinary)
Turbidity
ISSN:2045-2322, 2045-2322
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
AbstractList Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
Abstract Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and a C-terminal transmembrane domain. The catalytic domain of the endolysin belongs to the conserved protein family PHA02564 which has no recognizable sequence similarity to other known endolysin types. Turbidity reduction assays indicate that the Enc34 enzyme is active against peptidoglycan from a variety of Gram-negative bacteria including the opportunistic pathogen Pseudomonas aeruginosa PAO1. The crystal structure of the catalytic domain of the Enc34 endolysin shows a distinctive all-helical architecture that distantly resembles the α-lobe of the lysozyme fold. Conserved catalytically important residues suggest a shared evolutionary history between the Enc34 endolysin and GH73 and GH23 family glycoside hydrolases and propose a molecular signature for substrate cleavage for a large group of peptidoglycan-degrading enzymes.
ArticleNumber 5005
Author Cernooka, Elina
Tars, Kaspars
Zrelovs, Nikita
Kazaks, Andris
Rumnieks, Janis
Author_xml – sequence: 1
  givenname: Elina
  surname: Cernooka
  fullname: Cernooka, Elina
  organization: Latvian Biomedical Research and Study Centre
– sequence: 2
  givenname: Janis
  surname: Rumnieks
  fullname: Rumnieks, Janis
  organization: Latvian Biomedical Research and Study Centre
– sequence: 3
  givenname: Nikita
  surname: Zrelovs
  fullname: Zrelovs, Nikita
  organization: Latvian Biomedical Research and Study Centre
– sequence: 4
  givenname: Kaspars
  surname: Tars
  fullname: Tars, Kaspars
  organization: Latvian Biomedical Research and Study Centre, Faculty of Biology, University of Latvia
– sequence: 5
  givenname: Andris
  surname: Kazaks
  fullname: Kazaks, Andris
  email: andris@biomed.lu.lv
  organization: Latvian Biomedical Research and Study Centre
BackLink https://www.ncbi.nlm.nih.gov/pubmed/35322067$$D View this record in MEDLINE/PubMed
BookMark eNp9Uk1v1DAQjVARLaV_gAOyxIVLij_ixOGAVJVSKlXiAmdrYk92s0rsxXYqhV-Pu9uWtof6YmvmvTdvxvO2OHDeYVG8Z_SUUaE-x4rJVpWU85KqppYle1UccVrJkgvODx69D4uTGDc0H8nbirVvikMhc5zWzVERvg03GOKQFuJ7ktZIxiX6v8uEpPej_UJiCrNJc8D7vIEE45IGQ6yfYHCkD34i4Mjs5jjDSNBZn0VyBp3xFi3pFrJdwwrJhTOiele87mGMeHJ3Hxe_v1_8Ov9RXv-8vDo_uy5N1dBUtlT2WCtZM2yQQguUGwCOgvZtk9vuKmWbDphgUnYtAnS2rYS0naml6iiK4-Jqr2s9bPQ2DBOERXsY9C7gw0pDyH2MqOvWyp4p7IDLCpEDrS01PBe0LbWtyVpf91rbuZvQGnQpwPhE9GnGDWu98jdaZU9Uyizw6U4g-D8zxqSnIRocR3Do56h5XXGlpKpUhn58Bt34Obg8qh2KqVrUIqM-PHb0YOX-azOA7wEm-BgD9g8QRvXtCun9Cuk8S71bIc0yST0jmSFBGvxtV8P4MlXsqTHXcSsM_22_wPoHb4rb5A
CitedBy_id crossref_primary_10_1016_j_biotechadv_2023_108116
crossref_primary_10_1016_j_bbapap_2023_140918
crossref_primary_10_3390_v14091842
crossref_primary_10_3390_ijms251910838
crossref_primary_10_3390_molecules29225386
crossref_primary_10_1038_s44319_024_00060_6
crossref_primary_10_1002_1873_3468_70042
crossref_primary_10_1093_femsle_fnae103
crossref_primary_10_1186_s12866_023_02832_x
crossref_primary_10_3390_cryst15050448
crossref_primary_10_1186_s12866_025_03884_x
Cites_doi 10.1093/nar/gkw408
10.1107/S0907444909047337
10.1057/s41599-020-0478-4
10.1038/s41598-018-37417-6
10.1007/s00253-011-3104-y
10.1107/S0907444910007493
10.1073/pnas.0400957101
10.1007/s00253-003-1522-1
10.1093/molbev/msaa015
10.3390/antibiotics9040155
10.1007/978-1-0716-1290-3_23
10.1046/j.1365-2958.1999.01501.x
10.3389/fmicb.2018.01033
10.2217/fmb.15.8
10.4161/bact.1.1.14868
10.1107/S1600576716004416
10.1002/pro.3330
10.3389/fmicb.2021.748718
10.1007/s12275-014-4087-z
10.3390/v11030268
10.1002/pro.3749
10.1093/glycob/cwu113
10.1016/j.biotechadv.2017.12.009
10.1111/mmi.14134
10.1093/molbev/mst024
10.1186/s12859-018-2342-8
10.1128/MRA.00188-19
10.1016/j.ijantimicag.2019.11.001
10.1038/s41587-019-0036-z
10.1038/nmeth.4285
10.1016/j.jbbm.2006.10.009
10.1016/S1473-3099(20)30327-3
10.1107/S0021889807021206
10.1074/jbc.M709398200
10.1107/S0907444911001314
10.1128/JVI.01954-12
10.1038/s41564-019-0531-5
10.3390/molecules22071038
10.1006/jmbi.2000.4315
10.1007/s00018-004-4301-y
10.1038/nature10388
10.32607/20758251-2017-9-1-81-87
10.1093/nar/gki408
10.1107/S2059798319011471
10.3390/microorganisms8030447
10.1021/cb500439c
10.1093/nar/gkn201
10.1111/j.1574-6976.2007.00094.x
10.1038/msb.2011.75
10.2217/fmb.12.97
10.3390/v13040680
ContentType Journal Article
Copyright The Author(s) 2022
2022. The Author(s).
The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml – notice: The Author(s) 2022
– notice: 2022. The Author(s).
– notice: The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID C6C
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
3V.
7X7
7XB
88A
88E
88I
8FE
8FH
8FI
8FJ
8FK
ABUWG
AEUYN
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
FYUFA
GHDGH
GNUQQ
HCIFZ
K9.
LK8
M0S
M1P
M2P
M7P
PHGZM
PHGZT
PIMPY
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQQKQ
PQUKI
Q9U
7X8
5PM
DOA
DOI 10.1038/s41598-022-08765-1
DatabaseName Springer Nature OA Free Journals
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
ProQuest Central (Corporate)
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Biology Database (Alumni Edition)
Medical Database (Alumni Edition)
Science Database (Alumni Edition)
ProQuest SciTech Collection
ProQuest Natural Science Collection
ProQuest Hospital Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest One Sustainability (subscription)
ProQuest Central UK/Ireland
ProQuest Central Essentials - QC
Biological Science Collection
ProQuest Central
Natural Science Collection
ProQuest One
ProQuest Central
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
ProQuest Health & Medical Collection
PML(ProQuest Medical Library)
Science Database
Biological Science Database
ProQuest Central Premium
ProQuest One Academic (New)
Publicly Available Content Database
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
ProQuest One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic (retired)
ProQuest One Academic UKI Edition
ProQuest Central Basic
MEDLINE - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
Publicly Available Content Database
ProQuest Central Student
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Natural Science Collection
ProQuest Biology Journals (Alumni Edition)
ProQuest Central
ProQuest One Applied & Life Sciences
ProQuest One Sustainability
ProQuest Health & Medical Research Collection
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
Natural Science Collection
ProQuest Central Korea
Health & Medical Research Collection
Biological Science Collection
ProQuest Central (New)
ProQuest Medical Library (Alumni)
ProQuest Science Journals (Alumni Edition)
ProQuest Biological Science Collection
ProQuest Central Basic
ProQuest Science Journals
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
Biological Science Database
ProQuest SciTech Collection
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest One Academic (New)
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList
Publicly Available Content Database
MEDLINE

MEDLINE - Academic
CrossRef
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: NPM
  name: PubMed
  url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 3
  dbid: PIMPY
  name: Publicly Available Content Database
  url: http://search.proquest.com/publiccontent
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2045-2322
EndPage 11
ExternalDocumentID oai_doaj_org_article_69d5f18eba254ee2a06d0c22cad90d9c
PMC8943055
35322067
10_1038_s41598_022_08765_1
Genre Research Support, Non-U.S. Gov't
Journal Article
GrantInformation_xml – fundername: European Social Fund
  grantid: 8.2.2.0/20/I/006
  funderid: http://dx.doi.org/10.13039/501100004895
– fundername: SIA “Mikrotīkls”
– fundername: ;
– fundername: ;
  grantid: 8.2.2.0/20/I/006
GroupedDBID 0R~
3V.
4.4
53G
5VS
7X7
88A
88E
88I
8FE
8FH
8FI
8FJ
AAFWJ
AAJSJ
AAKDD
ABDBF
ABUWG
ACGFS
ACSMW
ACUHS
ADBBV
ADRAZ
AENEX
AEUYN
AFKRA
AJTQC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
C6C
CCPQU
DIK
DWQXO
EBD
EBLON
EBS
ESX
FYUFA
GNUQQ
GROUPED_DOAJ
GX1
HCIFZ
HH5
HMCUK
HYE
KQ8
LK8
M0L
M1P
M2P
M48
M7P
M~E
NAO
OK1
PIMPY
PQQKQ
PROAC
PSQYO
RNT
RNTTT
RPM
SNYQT
UKHRP
AASML
AAYXX
AFFHD
AFPKN
CITATION
PHGZM
PHGZT
PJZUB
PPXIY
PQGLB
CGR
CUY
CVF
ECM
EIF
NPM
7XB
8FK
K9.
PKEHL
PQEST
PQUKI
Q9U
7X8
5PM
ID FETCH-LOGICAL-c470t-905fe68561e7e0a9a02caa2e30f97022b48d7ba13155b9eaabd9435dbc658b0e3
IEDL.DBID BENPR
ISICitedReferencesCount 11
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000772605500123&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 2045-2322
IngestDate Tue Oct 14 14:59:15 EDT 2025
Tue Nov 04 01:58:38 EST 2025
Sun Nov 09 14:28:20 EST 2025
Tue Oct 07 07:41:20 EDT 2025
Wed Apr 16 06:21:38 EDT 2025
Tue Nov 18 21:43:58 EST 2025
Sat Nov 29 06:25:41 EST 2025
Fri Feb 21 02:39:01 EST 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License 2022. The Author(s).
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c470t-905fe68561e7e0a9a02caa2e30f97022b48d7ba13155b9eaabd9435dbc658b0e3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
OpenAccessLink https://www.proquest.com/docview/2642186363?pq-origsite=%requestingapplication%
PMID 35322067
PQID 2642186363
PQPubID 2041939
PageCount 11
ParticipantIDs doaj_primary_oai_doaj_org_article_69d5f18eba254ee2a06d0c22cad90d9c
pubmedcentral_primary_oai_pubmedcentral_nih_gov_8943055
proquest_miscellaneous_2642885848
proquest_journals_2642186363
pubmed_primary_35322067
crossref_primary_10_1038_s41598_022_08765_1
crossref_citationtrail_10_1038_s41598_022_08765_1
springer_journals_10_1038_s41598_022_08765_1
PublicationCentury 2000
PublicationDate 2022-03-23
PublicationDateYYYYMMDD 2022-03-23
PublicationDate_xml – month: 03
  year: 2022
  text: 2022-03-23
  day: 23
PublicationDecade 2020
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationTitle Scientific reports
PublicationTitleAbbrev Sci Rep
PublicationTitleAlternate Sci Rep
PublicationYear 2022
Publisher Nature Publishing Group UK
Nature Publishing Group
Nature Portfolio
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
– name: Nature Portfolio
References SieversFFast, scalable generation of high-quality protein multiple sequence alignments using Clustal OmegaMol. Syst. Biol.2011753921988835326169910.1038/msb.2011.75
BriersYLavigneRVolckaertGHertveldtKA standardized approach for accurate quantification of murein hydrolase activity in high-throughput assaysJ. Biochem. Biophys. Methods2007705315331:CAS:528:DC%2BD2sXislKjtLo%3D1716943510.1016/j.jbbm.2006.10.009
VasinaDVDiscovering the potentials of four phage endolysins to combat Gram-negative infectionsFront. Microbiol.20211234721353854876910.3389/fmicb.2021.748718
OritoYMoritaMHoriKUnnoHTanjiYBacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysisAppl. Microbiol. Biotechnol.2004651051091:CAS:528:DC%2BD2cXkvF2mt7c%3D1471415110.1007/s00253-003-1522-1
Interagency Coordination Group on Antimicrobial Resistance. No time to wait: Securing the future from drug-resistant infections report to the Secretary-General of the United Nations. https://www.who.int/antimicrobial-resistance/interagency-coordination-group/IACG_final_report_EN.pdf?ua=1 (Accessed 30 Oct 2021) (2019).
MurshudovGNREFMAC5 for the refinement of macromolecular crystal structuresActa Crystallogr. D Biol. Crystallogr.2011673553671:CAS:528:DC%2BC3MXktFWqtbk%3D21460454306975110.1107/S0907444911001314
Fernández-RuizICoutinhoFHRodriguez-ValeraFThousands of novel endolysins discovered in uncultured phage genomesFront. Microbiol.20189103329867909596886410.3389/fmicb.2018.01033
SpiwokVCH/π interactions in carbohydrate recognitionMolecules2017221038615232010.3390/molecules22071038
WaglechnerNMcArthurAGWrightGDPhylogenetic reconciliation reveals the natural history of glycopeptide antibiotic biosynthesis and resistanceNat. Microbiol.20194186218711:CAS:528:DC%2BC1MXhsFKhtbbL3140633410.1038/s41564-019-0531-5
Rambaut, A. FigTree v. 1.4.4. http://tree.bio.ed.ac.uk/software/figtree/ (2018).
ChertkovOVDual active site in the endolytic transglycosylase gp144 of bacteriophage phiKZActa Nat.2017981871:STN:280:DC%2BC1crjtVKjug%3D%3D10.32607/20758251-2017-9-1-81-87
BriersYPeetersLMVolckaertGLavigneRThe lysis cassette of bacteriophage ϕKMV encodes a signal-arrest-release endolysin and a pinholinBacteriophage20111253021687532310945110.4161/bact.1.1.14868
SchmelcherMDonovanDMLoessnerMJBacteriophage endolysins as novel antimicrobialsFuture Microbiol.20127114711711:CAS:528:DC%2BC38XhsVCjtb7F2303042210.2217/fmb.12.97
SpartaKMKrugMHeinemannUMuellerUWeissMSXDSAPP2.0J. Appl. Crystallogr.2016491085109210.1107/S1600576716004416
WilliamsCJMolProbity: More and better reference data for improved all-atom structure validationProtein Sci.2018272933151:CAS:528:DC%2BC2sXhvVKgsrnO2906776610.1002/pro.3330
KabschWXDSActa Crystallogr. D Biol. Crystallogr.2010661251321:CAS:528:DC%2BC3cXhs1SisLc%3D20124692281566510.1107/S0907444909047337
LiebschnerDMacromolecular structure determination using X-rays, neutrons and electrons: Recent developments in PhenixActa Crystallogr. D Struct. Biol.2019758618771:CAS:528:DC%2BC1MXhvFWkurrO31588918677885210.1107/S2059798319011471
GraschopfABläsiUMolecular function of the dual-start motif in the lambda S holinMol. Microbiol.1999335695821:CAS:528:DyaK1MXlslSjur4%3D1041764710.1046/j.1365-2958.1999.01501.x
FokineAMiroshnikovKAShneiderMMMesyanzhinovVVRossmannMGStructure of the bacteriophage phiKZ lytic transglycosylase gp144J. Biol. Chem.2008283724275501:CAS:528:DC%2BD1cXivFyisr8%3D1816039410.1074/jbc.M709398200
EmsleyPLohkampBScottWGCowtanKFeatures and development of CootActa Crystallogr. D Biol. Crystallogr.2010664865011:CAS:528:DC%2BC3cXksFKisb8%3D20383002285231310.1107/S0907444910007493
YoungRPhage lysis: Three steps, three choices, one outcomeJ. Microbiol.2014522432581:CAS:528:DC%2BC2cXjs1Gisbc%3D24585055401243110.1007/s12275-014-4087-z
MinhBQIQ-TREE 2: New models and efficient methods for phylogenetic inference in the genomic eraMol. Biol. Evol.202037153015341:CAS:528:DC%2BB3cXis1egsLbL32011700718220610.1093/molbev/msaa015
LavigneRBriersYHertveldtKRobbenJVolckaertGIdentification and characterization of a highly thermostable bacteriophage lysozymeCell. Mol. Life Sci.200461275327591:CAS:528:DC%2BD2cXhtFGit7vN1554917810.1007/s00018-004-4301-y
MurrayEDraperLARossRPHillCThe advantages and challenges of using endolysins in a clinical settingViruses2021136801:CAS:528:DC%2BB3MXhtVSjsrrE33920965807125910.3390/v13040680
LaiMJAntibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteriaAppl. Microbiol. Biotechnol.2011905295391:CAS:528:DC%2BC3MXjsFGhs7Y%3D2126446610.1007/s00253-011-3104-y
KimBOPhage-derived antibacterials: Harnessing the simplicity, plasticity, and diversity of phagesViruses2019112681:CAS:528:DC%2BC1MXhslymur3J646613010.3390/v11030268
LipskiAStructural and biochemical characterization of the β-N-acetylglucosaminidase from Thermotoga maritima: Toward rationalization of mechanistic knowledge in the GH73 familyGlycobiology2015253193301:CAS:528:DC%2BC28Xht1Wqu77O2534444510.1093/glycob/cwu113
SödingJBiegertALupasANThe HHpred interactive server for protein homology detection and structure predictionNucleic Acids Res.200533W244W24815980461116016910.1093/nar/gki408
MinhBQNguyenMAvon HaeselerAUltrafast approximation for phylogenetic bootstrapMol. Biol. Evol.201330118811951:CAS:528:DC%2BC3sXlvFWgsb0%3D23418397367074110.1093/molbev/mst024
VentolaCLThe antibiotic resistance crisis: Part 2: Management strategies and new agentsP T201540344352259878234422635
JohnsonMNCBI BLAST: A better web interfaceNucleic Acids Res.200836W5W91:CAS:528:DC%2BD1cXptlKrs70%3D18440982244771610.1093/nar/gkn201
McCoyAJPhaser crystallographic softwareJ. Appl. Crystallogr.2007406586741:CAS:528:DC%2BD2sXnslWqsLk%3D19461840248347210.1107/S0021889807021206
D’CostaVMAntibiotic resistance is ancientNature2011477457461218815612011Natur.477..457D10.1038/nature10388
KazaksADislersALipowskyGNikolajevaVTarsKComplete genome sequence of the Enterobacter cancerogenus bacteriophage Enc34J. Virol.20128611403114041:CAS:528:DC%2BC38XhsVyqsr3I22997422345718510.1128/JVI.01954-12
BriersYLavigneRBreaking barriers: Expansion of the use of endolysins as novel antibacterials against Gram-negative bacteriaFuture Microbiol.2015103773901:CAS:528:DC%2BC2MXltlCrsLw%3D2581246110.2217/fmb.15.8
MaganaMThe value of antimicrobial peptides in the age of resistanceLancet Infect. Dis.202020e216e2301:CAS:528:DC%2BB3cXhtl2rsLrK3265307010.1016/S1473-3099(20)30327-3
BaiJLeeSRyuSIdentification and in vitro characterization of a novel phage endolysin that targets Gram-negative bacteriaMicroorganisms202084471:CAS:528:DC%2BB3cXhsVWjsLfE714399210.3390/microorganisms8030447
KroghALarssonBvon HeijneGSonnhammerELPredicting transmembrane protein topology with a hidden Markov model: Application to complete genomesJ. Mol. Biol.20013055675801:CAS:528:DC%2BD3MXisFCguw%3D%3D1115261310.1006/jmbi.2000.4315
VollmerWBlanotDde PedroMAPeptidoglycan structure and architectureFEMS Microbiol. Rev.2008321491671:CAS:528:DC%2BD1cXjt1Git7k%3D1819433610.1111/j.1574-6976.2007.00094.x
BrivesCPourrazJPhage therapy as a potential solution in the fight against AMR: Obstacles and possible futuresPalgrave Commun.2020610010.1057/s41599-020-0478-4
O’LearyCXieYKongariRGillJJLiuMComplete genome sequence of Salmonella enterica serovar Typhimurium siphophage SiskinMicrobiol. Resour. Announc.20198e00188e21931048394649822710.1128/MRA.00188-19
PlotkaMStructure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan bindingSci. Rep.2019912613071861163619862019NatSR...9.1261P10.1038/s41598-018-37417-6
KalyaanamoorthySMinhBQWongTvon HaeselerAJermiinLSModelFinder: Fast model selection for accurate phylogenetic estimatesNat. Methods2017145875891:CAS:528:DC%2BC2sXntFKitbw%3D28481363545324510.1038/nmeth.4285
Schrödinger, L. & DeLano, W. PyMOL. http://www.pymol.org/pymol (2020).
ZurawskiDVMcLendonMKMonoclonal antibodies as an antibacterial approach against bacterial pathogensAntibiotics (Basel)202091551:CAS:528:DC%2BB3cXitF2ht77N10.3390/antibiotics9040155
BroendumSSBuckleAMMcGowanSCatalytic diversity and cell wall binding repeats in the phage-encoded endolysinsMol. Microbiol.20181108798961:CAS:528:DC%2BC1cXitFOis7jK3023064210.1111/mmi.14134
HolmLDALI and the persistence of protein shapeProtein Sci.2020291281401:CAS:528:DC%2BC1MXitFWjsbzO3160689410.1002/pro.3749
KongariRPhage spanins: Diversity, topological dynamics and gene convergenceBMC Bioinform.2018193261:CAS:528:DC%2BC1MXht1Sks7%2FO10.1186/s12859-018-2342-8
GerstmansHCrielBBriersYSynthetic biology of modular endolysinsBiotechnol. Adv.2018366246401:CAS:528:DC%2BC1cXkvFyhtg%3D%3D2924868210.1016/j.biotechadv.2017.12.009
XuMStruckDKDeatonJWangINYoungRA signal-arrest-release sequence mediates export and control of the phage P1 endolysinProc. Natl. Acad. Sci. U.S.A.2004101641564201:CAS:528:DC%2BD2cXjvVyit7k%3D150906504040592004PNAS..101.6415X10.1073/pnas.0400957101
CernookaERumnieksJKazaksAStructural characterization of a single-stranded DNA-binding protein: A case study of the ORF6 protein from bacteriophage Enc34Methods Mol. Biol.202122813433731:CAS:528:DC%2BB3MXisFals7%2FK3384797110.1007/978-1-0716-1290-3_23
GondilVSHarjaiKChhibberSEndolysins as emerging alternative therapeutic agents to counter drug-resistant infectionsInt. J. Antimicrob. Agents2020551:CAS:528:DC%2BB3cXht1Sit7c%3D3171525710.1016/j.ijantimicag.2019.11.001
AshkenazyHConSurf 2016: An improved methodology to estimate and visualize evolutionary conservation in macromoleculesNucleic Acids Res.201644W344W3501:CAS:528:DC%2BC2sXhtV2itrrJ27166375498794010.1093/nar/gkw408
Artola-RecolonsCStructure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coliACS Chem. Biol.20149205820661:CAS:528:DC%2BC2cXhtVyitLzK24988330416878310.1021/cb500439c
Almagro ArmenterosJJSignalP 5.0 improves signal peptide predictions using deep neural networksNat. Biotechnol.2019374204231:CAS:528:DC%2BC1MXosV2qs78%3
D Liebschner (8765_CR51) 2019; 75
CL Ventola (8765_CR4) 2015; 40
W Vollmer (8765_CR23) 2008; 32
L Holm (8765_CR25) 2020; 29
V Spiwok (8765_CR37) 2017; 22
Y Briers (8765_CR15) 2015; 10
M Plotka (8765_CR32) 2019; 9
GN Murshudov (8765_CR53) 2011; 67
OV Chertkov (8765_CR28) 2017; 9
H Gerstmans (8765_CR13) 2018; 36
BQ Minh (8765_CR43) 2020; 37
8765_CR1
SS Broendum (8765_CR14) 2018; 110
J Söding (8765_CR39) 2005; 33
A Kazaks (8765_CR19) 2012; 86
R Kongari (8765_CR21) 2018; 19
C Artola-Recolons (8765_CR36) 2014; 9
I Fernández-Ruiz (8765_CR18) 2018; 9
A Graschopf (8765_CR20) 1999; 33
BO Kim (8765_CR7) 2019; 11
8765_CR24
C O’Leary (8765_CR29) 2019; 8
VS Gondil (8765_CR12) 2020; 55
M Magana (8765_CR5) 2020; 20
Y Orito (8765_CR31) 2004; 65
N Waglechner (8765_CR2) 2019; 4
E Cernooka (8765_CR47) 2021; 2281
CJ Williams (8765_CR55) 2018; 27
C Brives (8765_CR8) 2020; 6
R Young (8765_CR33) 2014; 52
A Lipski (8765_CR27) 2015; 25
P Emsley (8765_CR52) 2010; 66
E Murray (8765_CR9) 2021; 13
Y Briers (8765_CR22) 2007; 70
DV Zurawski (8765_CR6) 2020; 9
VM D’Costa (8765_CR3) 2011; 477
M Johnson (8765_CR38) 2008; 36
JJ Almagro Armenteros (8765_CR41) 2019; 37
DV Vasina (8765_CR11) 2021; 12
M Schmelcher (8765_CR10) 2012; 7
J Bai (8765_CR30) 2020; 8
KM Sparta (8765_CR50) 2016; 49
Y Briers (8765_CR34) 2011; 1
A Fokine (8765_CR35) 2008; 283
S Kalyaanamoorthy (8765_CR44) 2017; 14
8765_CR46
R Lavigne (8765_CR48) 2004; 61
W Kabsch (8765_CR49) 2010; 66
MJ Lai (8765_CR17) 2011; 90
H Ashkenazy (8765_CR26) 2016; 44
BQ Minh (8765_CR45) 2013; 30
AJ McCoy (8765_CR54) 2007; 40
A Krogh (8765_CR40) 2001; 305
F Sievers (8765_CR42) 2011; 7
M Xu (8765_CR16) 2004; 101
References_xml – reference: MaganaMThe value of antimicrobial peptides in the age of resistanceLancet Infect. Dis.202020e216e2301:CAS:528:DC%2BB3cXhtl2rsLrK3265307010.1016/S1473-3099(20)30327-3
– reference: LavigneRBriersYHertveldtKRobbenJVolckaertGIdentification and characterization of a highly thermostable bacteriophage lysozymeCell. Mol. Life Sci.200461275327591:CAS:528:DC%2BD2cXhtFGit7vN1554917810.1007/s00018-004-4301-y
– reference: McCoyAJPhaser crystallographic softwareJ. Appl. Crystallogr.2007406586741:CAS:528:DC%2BD2sXnslWqsLk%3D19461840248347210.1107/S0021889807021206
– reference: MurrayEDraperLARossRPHillCThe advantages and challenges of using endolysins in a clinical settingViruses2021136801:CAS:528:DC%2BB3MXhtVSjsrrE33920965807125910.3390/v13040680
– reference: KroghALarssonBvon HeijneGSonnhammerELPredicting transmembrane protein topology with a hidden Markov model: Application to complete genomesJ. Mol. Biol.20013055675801:CAS:528:DC%2BD3MXisFCguw%3D%3D1115261310.1006/jmbi.2000.4315
– reference: EmsleyPLohkampBScottWGCowtanKFeatures and development of CootActa Crystallogr. D Biol. Crystallogr.2010664865011:CAS:528:DC%2BC3cXksFKisb8%3D20383002285231310.1107/S0907444910007493
– reference: WaglechnerNMcArthurAGWrightGDPhylogenetic reconciliation reveals the natural history of glycopeptide antibiotic biosynthesis and resistanceNat. Microbiol.20194186218711:CAS:528:DC%2BC1MXhsFKhtbbL3140633410.1038/s41564-019-0531-5
– reference: XuMStruckDKDeatonJWangINYoungRA signal-arrest-release sequence mediates export and control of the phage P1 endolysinProc. Natl. Acad. Sci. U.S.A.2004101641564201:CAS:528:DC%2BD2cXjvVyit7k%3D150906504040592004PNAS..101.6415X10.1073/pnas.0400957101
– reference: VentolaCLThe antibiotic resistance crisis: Part 2: Management strategies and new agentsP T201540344352259878234422635
– reference: ZurawskiDVMcLendonMKMonoclonal antibodies as an antibacterial approach against bacterial pathogensAntibiotics (Basel)202091551:CAS:528:DC%2BB3cXitF2ht77N10.3390/antibiotics9040155
– reference: D’CostaVMAntibiotic resistance is ancientNature2011477457461218815612011Natur.477..457D10.1038/nature10388
– reference: MurshudovGNREFMAC5 for the refinement of macromolecular crystal structuresActa Crystallogr. D Biol. Crystallogr.2011673553671:CAS:528:DC%2BC3MXktFWqtbk%3D21460454306975110.1107/S0907444911001314
– reference: Almagro ArmenterosJJSignalP 5.0 improves signal peptide predictions using deep neural networksNat. Biotechnol.2019374204231:CAS:528:DC%2BC1MXosV2qs78%3D3077823310.1038/s41587-019-0036-z
– reference: YoungRPhage lysis: Three steps, three choices, one outcomeJ. Microbiol.2014522432581:CAS:528:DC%2BC2cXjs1Gisbc%3D24585055401243110.1007/s12275-014-4087-z
– reference: BroendumSSBuckleAMMcGowanSCatalytic diversity and cell wall binding repeats in the phage-encoded endolysinsMol. Microbiol.20181108798961:CAS:528:DC%2BC1cXitFOis7jK3023064210.1111/mmi.14134
– reference: SpiwokVCH/π interactions in carbohydrate recognitionMolecules2017221038615232010.3390/molecules22071038
– reference: O’LearyCXieYKongariRGillJJLiuMComplete genome sequence of Salmonella enterica serovar Typhimurium siphophage SiskinMicrobiol. Resour. Announc.20198e00188e21931048394649822710.1128/MRA.00188-19
– reference: OritoYMoritaMHoriKUnnoHTanjiYBacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysisAppl. Microbiol. Biotechnol.2004651051091:CAS:528:DC%2BD2cXkvF2mt7c%3D1471415110.1007/s00253-003-1522-1
– reference: SpartaKMKrugMHeinemannUMuellerUWeissMSXDSAPP2.0J. Appl. Crystallogr.2016491085109210.1107/S1600576716004416
– reference: SchmelcherMDonovanDMLoessnerMJBacteriophage endolysins as novel antimicrobialsFuture Microbiol.20127114711711:CAS:528:DC%2BC38XhsVCjtb7F2303042210.2217/fmb.12.97
– reference: BriersYLavigneRVolckaertGHertveldtKA standardized approach for accurate quantification of murein hydrolase activity in high-throughput assaysJ. Biochem. Biophys. Methods2007705315331:CAS:528:DC%2BD2sXislKjtLo%3D1716943510.1016/j.jbbm.2006.10.009
– reference: KabschWXDSActa Crystallogr. D Biol. Crystallogr.2010661251321:CAS:528:DC%2BC3cXhs1SisLc%3D20124692281566510.1107/S0907444909047337
– reference: Fernández-RuizICoutinhoFHRodriguez-ValeraFThousands of novel endolysins discovered in uncultured phage genomesFront. Microbiol.20189103329867909596886410.3389/fmicb.2018.01033
– reference: PlotkaMStructure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan bindingSci. Rep.2019912613071861163619862019NatSR...9.1261P10.1038/s41598-018-37417-6
– reference: BrivesCPourrazJPhage therapy as a potential solution in the fight against AMR: Obstacles and possible futuresPalgrave Commun.2020610010.1057/s41599-020-0478-4
– reference: JohnsonMNCBI BLAST: A better web interfaceNucleic Acids Res.200836W5W91:CAS:528:DC%2BD1cXptlKrs70%3D18440982244771610.1093/nar/gkn201
– reference: VasinaDVDiscovering the potentials of four phage endolysins to combat Gram-negative infectionsFront. Microbiol.20211234721353854876910.3389/fmicb.2021.748718
– reference: SieversFFast, scalable generation of high-quality protein multiple sequence alignments using Clustal OmegaMol. Syst. Biol.2011753921988835326169910.1038/msb.2011.75
– reference: WilliamsCJMolProbity: More and better reference data for improved all-atom structure validationProtein Sci.2018272933151:CAS:528:DC%2BC2sXhvVKgsrnO2906776610.1002/pro.3330
– reference: Schrödinger, L. & DeLano, W. PyMOL. http://www.pymol.org/pymol (2020).
– reference: MinhBQIQ-TREE 2: New models and efficient methods for phylogenetic inference in the genomic eraMol. Biol. Evol.202037153015341:CAS:528:DC%2BB3cXis1egsLbL32011700718220610.1093/molbev/msaa015
– reference: Interagency Coordination Group on Antimicrobial Resistance. No time to wait: Securing the future from drug-resistant infections report to the Secretary-General of the United Nations. https://www.who.int/antimicrobial-resistance/interagency-coordination-group/IACG_final_report_EN.pdf?ua=1 (Accessed 30 Oct 2021) (2019).
– reference: BaiJLeeSRyuSIdentification and in vitro characterization of a novel phage endolysin that targets Gram-negative bacteriaMicroorganisms202084471:CAS:528:DC%2BB3cXhsVWjsLfE714399210.3390/microorganisms8030447
– reference: SödingJBiegertALupasANThe HHpred interactive server for protein homology detection and structure predictionNucleic Acids Res.200533W244W24815980461116016910.1093/nar/gki408
– reference: KimBOPhage-derived antibacterials: Harnessing the simplicity, plasticity, and diversity of phagesViruses2019112681:CAS:528:DC%2BC1MXhslymur3J646613010.3390/v11030268
– reference: MinhBQNguyenMAvon HaeselerAUltrafast approximation for phylogenetic bootstrapMol. Biol. Evol.201330118811951:CAS:528:DC%2BC3sXlvFWgsb0%3D23418397367074110.1093/molbev/mst024
– reference: LipskiAStructural and biochemical characterization of the β-N-acetylglucosaminidase from Thermotoga maritima: Toward rationalization of mechanistic knowledge in the GH73 familyGlycobiology2015253193301:CAS:528:DC%2BC28Xht1Wqu77O2534444510.1093/glycob/cwu113
– reference: VollmerWBlanotDde PedroMAPeptidoglycan structure and architectureFEMS Microbiol. Rev.2008321491671:CAS:528:DC%2BD1cXjt1Git7k%3D1819433610.1111/j.1574-6976.2007.00094.x
– reference: Rambaut, A. FigTree v. 1.4.4. http://tree.bio.ed.ac.uk/software/figtree/ (2018).
– reference: FokineAMiroshnikovKAShneiderMMMesyanzhinovVVRossmannMGStructure of the bacteriophage phiKZ lytic transglycosylase gp144J. Biol. Chem.2008283724275501:CAS:528:DC%2BD1cXivFyisr8%3D1816039410.1074/jbc.M709398200
– reference: GondilVSHarjaiKChhibberSEndolysins as emerging alternative therapeutic agents to counter drug-resistant infectionsInt. J. Antimicrob. Agents2020551:CAS:528:DC%2BB3cXht1Sit7c%3D3171525710.1016/j.ijantimicag.2019.11.001
– reference: BriersYLavigneRBreaking barriers: Expansion of the use of endolysins as novel antibacterials against Gram-negative bacteriaFuture Microbiol.2015103773901:CAS:528:DC%2BC2MXltlCrsLw%3D2581246110.2217/fmb.15.8
– reference: LaiMJAntibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteriaAppl. Microbiol. Biotechnol.2011905295391:CAS:528:DC%2BC3MXjsFGhs7Y%3D2126446610.1007/s00253-011-3104-y
– reference: BriersYPeetersLMVolckaertGLavigneRThe lysis cassette of bacteriophage ϕKMV encodes a signal-arrest-release endolysin and a pinholinBacteriophage20111253021687532310945110.4161/bact.1.1.14868
– reference: GraschopfABläsiUMolecular function of the dual-start motif in the lambda S holinMol. Microbiol.1999335695821:CAS:528:DyaK1MXlslSjur4%3D1041764710.1046/j.1365-2958.1999.01501.x
– reference: LiebschnerDMacromolecular structure determination using X-rays, neutrons and electrons: Recent developments in PhenixActa Crystallogr. D Struct. Biol.2019758618771:CAS:528:DC%2BC1MXhvFWkurrO31588918677885210.1107/S2059798319011471
– reference: KongariRPhage spanins: Diversity, topological dynamics and gene convergenceBMC Bioinform.2018193261:CAS:528:DC%2BC1MXht1Sks7%2FO10.1186/s12859-018-2342-8
– reference: KazaksADislersALipowskyGNikolajevaVTarsKComplete genome sequence of the Enterobacter cancerogenus bacteriophage Enc34J. Virol.20128611403114041:CAS:528:DC%2BC38XhsVyqsr3I22997422345718510.1128/JVI.01954-12
– reference: HolmLDALI and the persistence of protein shapeProtein Sci.2020291281401:CAS:528:DC%2BC1MXitFWjsbzO3160689410.1002/pro.3749
– reference: KalyaanamoorthySMinhBQWongTvon HaeselerAJermiinLSModelFinder: Fast model selection for accurate phylogenetic estimatesNat. Methods2017145875891:CAS:528:DC%2BC2sXntFKitbw%3D28481363545324510.1038/nmeth.4285
– reference: Artola-RecolonsCStructure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coliACS Chem. Biol.20149205820661:CAS:528:DC%2BC2cXhtVyitLzK24988330416878310.1021/cb500439c
– reference: AshkenazyHConSurf 2016: An improved methodology to estimate and visualize evolutionary conservation in macromoleculesNucleic Acids Res.201644W344W3501:CAS:528:DC%2BC2sXhtV2itrrJ27166375498794010.1093/nar/gkw408
– reference: ChertkovOVDual active site in the endolytic transglycosylase gp144 of bacteriophage phiKZActa Nat.2017981871:STN:280:DC%2BC1crjtVKjug%3D%3D10.32607/20758251-2017-9-1-81-87
– reference: GerstmansHCrielBBriersYSynthetic biology of modular endolysinsBiotechnol. Adv.2018366246401:CAS:528:DC%2BC1cXkvFyhtg%3D%3D2924868210.1016/j.biotechadv.2017.12.009
– reference: CernookaERumnieksJKazaksAStructural characterization of a single-stranded DNA-binding protein: A case study of the ORF6 protein from bacteriophage Enc34Methods Mol. Biol.202122813433731:CAS:528:DC%2BB3MXisFals7%2FK3384797110.1007/978-1-0716-1290-3_23
– volume: 44
  start-page: W344
  year: 2016
  ident: 8765_CR26
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw408
– ident: 8765_CR46
– volume: 66
  start-page: 125
  year: 2010
  ident: 8765_CR49
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444909047337
– volume: 6
  start-page: 100
  year: 2020
  ident: 8765_CR8
  publication-title: Palgrave Commun.
  doi: 10.1057/s41599-020-0478-4
– volume: 9
  start-page: 1261
  year: 2019
  ident: 8765_CR32
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-018-37417-6
– volume: 90
  start-page: 529
  year: 2011
  ident: 8765_CR17
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-011-3104-y
– volume: 66
  start-page: 486
  year: 2010
  ident: 8765_CR52
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444910007493
– volume: 101
  start-page: 6415
  year: 2004
  ident: 8765_CR16
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0400957101
– volume: 65
  start-page: 105
  year: 2004
  ident: 8765_CR31
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-003-1522-1
– volume: 37
  start-page: 1530
  year: 2020
  ident: 8765_CR43
  publication-title: Mol. Biol. Evol.
  doi: 10.1093/molbev/msaa015
– volume: 9
  start-page: 155
  year: 2020
  ident: 8765_CR6
  publication-title: Antibiotics (Basel)
  doi: 10.3390/antibiotics9040155
– volume: 2281
  start-page: 343
  year: 2021
  ident: 8765_CR47
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-0716-1290-3_23
– volume: 33
  start-page: 569
  year: 1999
  ident: 8765_CR20
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.1999.01501.x
– volume: 9
  start-page: 1033
  year: 2018
  ident: 8765_CR18
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2018.01033
– volume: 10
  start-page: 377
  year: 2015
  ident: 8765_CR15
  publication-title: Future Microbiol.
  doi: 10.2217/fmb.15.8
– volume: 1
  start-page: 25
  year: 2011
  ident: 8765_CR34
  publication-title: Bacteriophage
  doi: 10.4161/bact.1.1.14868
– volume: 49
  start-page: 1085
  year: 2016
  ident: 8765_CR50
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S1600576716004416
– volume: 27
  start-page: 293
  year: 2018
  ident: 8765_CR55
  publication-title: Protein Sci.
  doi: 10.1002/pro.3330
– volume: 12
  year: 2021
  ident: 8765_CR11
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2021.748718
– volume: 52
  start-page: 243
  year: 2014
  ident: 8765_CR33
  publication-title: J. Microbiol.
  doi: 10.1007/s12275-014-4087-z
– ident: 8765_CR1
– volume: 11
  start-page: 268
  year: 2019
  ident: 8765_CR7
  publication-title: Viruses
  doi: 10.3390/v11030268
– volume: 29
  start-page: 128
  year: 2020
  ident: 8765_CR25
  publication-title: Protein Sci.
  doi: 10.1002/pro.3749
– volume: 25
  start-page: 319
  year: 2015
  ident: 8765_CR27
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwu113
– volume: 36
  start-page: 624
  year: 2018
  ident: 8765_CR13
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2017.12.009
– volume: 110
  start-page: 879
  year: 2018
  ident: 8765_CR14
  publication-title: Mol. Microbiol.
  doi: 10.1111/mmi.14134
– volume: 30
  start-page: 1188
  year: 2013
  ident: 8765_CR45
  publication-title: Mol. Biol. Evol.
  doi: 10.1093/molbev/mst024
– volume: 19
  start-page: 326
  year: 2018
  ident: 8765_CR21
  publication-title: BMC Bioinform.
  doi: 10.1186/s12859-018-2342-8
– volume: 8
  start-page: e00188
  year: 2019
  ident: 8765_CR29
  publication-title: Microbiol. Resour. Announc.
  doi: 10.1128/MRA.00188-19
– volume: 55
  year: 2020
  ident: 8765_CR12
  publication-title: Int. J. Antimicrob. Agents
  doi: 10.1016/j.ijantimicag.2019.11.001
– volume: 37
  start-page: 420
  year: 2019
  ident: 8765_CR41
  publication-title: Nat. Biotechnol.
  doi: 10.1038/s41587-019-0036-z
– volume: 14
  start-page: 587
  year: 2017
  ident: 8765_CR44
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4285
– volume: 70
  start-page: 531
  year: 2007
  ident: 8765_CR22
  publication-title: J. Biochem. Biophys. Methods
  doi: 10.1016/j.jbbm.2006.10.009
– volume: 20
  start-page: e216
  year: 2020
  ident: 8765_CR5
  publication-title: Lancet Infect. Dis.
  doi: 10.1016/S1473-3099(20)30327-3
– volume: 40
  start-page: 658
  year: 2007
  ident: 8765_CR54
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
– volume: 283
  start-page: 7242
  year: 2008
  ident: 8765_CR35
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M709398200
– volume: 67
  start-page: 355
  year: 2011
  ident: 8765_CR53
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444911001314
– volume: 86
  start-page: 11403
  year: 2012
  ident: 8765_CR19
  publication-title: J. Virol.
  doi: 10.1128/JVI.01954-12
– volume: 4
  start-page: 1862
  year: 2019
  ident: 8765_CR2
  publication-title: Nat. Microbiol.
  doi: 10.1038/s41564-019-0531-5
– volume: 22
  start-page: 1038
  year: 2017
  ident: 8765_CR37
  publication-title: Molecules
  doi: 10.3390/molecules22071038
– ident: 8765_CR24
– volume: 305
  start-page: 567
  year: 2001
  ident: 8765_CR40
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2000.4315
– volume: 61
  start-page: 2753
  year: 2004
  ident: 8765_CR48
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-004-4301-y
– volume: 477
  start-page: 457
  year: 2011
  ident: 8765_CR3
  publication-title: Nature
  doi: 10.1038/nature10388
– volume: 9
  start-page: 81
  year: 2017
  ident: 8765_CR28
  publication-title: Acta Nat.
  doi: 10.32607/20758251-2017-9-1-81-87
– volume: 33
  start-page: W244
  year: 2005
  ident: 8765_CR39
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gki408
– volume: 75
  start-page: 861
  year: 2019
  ident: 8765_CR51
  publication-title: Acta Crystallogr. D Struct. Biol.
  doi: 10.1107/S2059798319011471
– volume: 8
  start-page: 447
  year: 2020
  ident: 8765_CR30
  publication-title: Microorganisms
  doi: 10.3390/microorganisms8030447
– volume: 40
  start-page: 344
  year: 2015
  ident: 8765_CR4
  publication-title: P T
– volume: 9
  start-page: 2058
  year: 2014
  ident: 8765_CR36
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb500439c
– volume: 36
  start-page: W5
  year: 2008
  ident: 8765_CR38
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkn201
– volume: 32
  start-page: 149
  year: 2008
  ident: 8765_CR23
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1111/j.1574-6976.2007.00094.x
– volume: 7
  start-page: 539
  year: 2011
  ident: 8765_CR42
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb.2011.75
– volume: 7
  start-page: 1147
  year: 2012
  ident: 8765_CR10
  publication-title: Future Microbiol.
  doi: 10.2217/fmb.12.97
– volume: 13
  start-page: 680
  year: 2021
  ident: 8765_CR9
  publication-title: Viruses
  doi: 10.3390/v13040680
SSID ssj0000529419
Score 2.4149413
Snippet Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections....
Abstract Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial...
SourceID doaj
pubmedcentral
proquest
pubmed
crossref
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 5005
SubjectTerms 631/337
631/535
Bacteria
Bacterial diseases
Bacteriophages - metabolism
Catalytic Domain
Conserved sequence
Crystal structure
Endopeptidases - metabolism
Enzymes
Glycoside hydrolase
Gram-negative bacteria
Humanities and Social Sciences
Lysozyme
multidisciplinary
Multidrug resistance
Muramidase - metabolism
Opportunist infection
Peptidoglycan - metabolism
Peptidoglycans
Phages
Science
Science (multidisciplinary)
Turbidity
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Jb9UwELZQBRIXxE5oQUbiBlGdOIvdG0srThUHkHqLvIzVJ7061UtTKfx6xnby6GO9cI2deDSL_Tkef0PIa9DWSWbbvK0alleaF7mCkPbHKqed5bWei020p6fi7Ex-vlHqK-SEJXrgpLjDRtraFQK0wq0MQKlYY5kpS6MsjiFNmH0R9dzYTCVW71JWhZxvyTAuDgdcqcJtMtx7BRa2Oi92VqJI2P87lPlrsuRPJ6ZxITq5T-7NCJK-S5I_ILfAPyR3Uk3J6RHZfFwyLWjvKMI7up6G_tt0AdT1a3tEE2PsuIGlPf7BmfBr1PYXauVpuHJClaejH4cRhwJv-8Bc4mlgvbRgqZ7o5TnORPTYG149Jl9Pjr98-JTPhRVyU7XsKpesdtAIhE7QAlNSMVSnKoEzJ1vUkK6EbbUqOIINLUEpbSXCKqsN4hXNgD8he7738IxQbhsn65KZtlSVAKel5fg9aArFG8VNRopFyZ2ZWcdD8Yt1F0-_ueiSYToctouG6YqMvNm-c5k4N_7a-32w3bZn4MuOD9CLutmLun95UUYOFst3cxAPXRkuAYuGNzwjr7bNGH7hTEV56MfURwhEcSIjT5OjbCXhNc6WiAYy0u640I6ouy1-dR4pviMrfl1n5O3ibD_E-rMqnv8PVeyTu2WMEp6X_IDsoVPCC3LbXF-ths3LGGbfAZEvLKE
  priority: 102
  providerName: Directory of Open Access Journals
Title Diversity of the lysozyme fold: structure of the catalytic domain from an unusual endolysin encoded by phage Enc34
URI https://link.springer.com/article/10.1038/s41598-022-08765-1
https://www.ncbi.nlm.nih.gov/pubmed/35322067
https://www.proquest.com/docview/2642186363
https://www.proquest.com/docview/2642885848
https://pubmed.ncbi.nlm.nih.gov/PMC8943055
https://doaj.org/article/69d5f18eba254ee2a06d0c22cad90d9c
Volume 12
WOSCitedRecordID wos000772605500123&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVAON
  databaseName: DOAJ Directory of Open Access Journals
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: DOA
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.doaj.org/
  providerName: Directory of Open Access Journals
– providerCode: PRVHPJ
  databaseName: ROAD: Directory of Open Access Scholarly Resources
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: M~E
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://road.issn.org
  providerName: ISSN International Centre
– providerCode: PRVPQU
  databaseName: Biological Science Database
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: M7P
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/biologicalscijournals
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Health & Medical Collection
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: 7X7
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/healthcomplete
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: BENPR
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Publicly Available Content Database
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: PIMPY
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: http://search.proquest.com/publiccontent
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: Science Database
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: M2P
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/sciencejournals
  providerName: ProQuest
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lj9MwELbYFiQuvB-BpTISN4jWiZPY5oJY6AoOW1UIpHKK7NhhK3Wd0myRwq9n7DhdlcdeuPgQO4mdGY-_zNjfIPTCKF0LolnMsoLEmaJJLI3b9keyWtWa5iokm2CzGV8sxDw43NqwrXKwid5Q66ZyPvKj1J3I5AUt6Jv199hljXLR1ZBC4wCNHVNZNkLj4-ls_mnnZXFxrCwR4bQMofyohRXLnSqDfzDHxpbHyd6K5In7_4Y2_9w0-Vvk1C9IJ7f_dyh30K0ARfHbXnfuomvG3kM3-uSU3X20eT9s2cBNjQEn4lXXNj-7c4PrZqVf4556drsxQ713BXXwNKybc7m02J1dwdLird22W3iVsbpxFCgWO_pMbTRWHV6fgUnDU1vR7AH6cjL9_O5DHDI0xFXGyEUsSF6bggMGM8wQKSRJKylTQ0ktGHxilXHNlEwooBYljJRKC8BnWlUAfBQx9CEa2caaxwhTXdQiT0nFUplxUyuhKTzPFImkhaRVhJJBSmUV6MtdFo1V6cPolJe9ZEt4beklWyYRerm7Z92Td1zZ-tgJf9fSEW_7C83mWxnmcVkIndcJN0rCn7UxqSSFJlUKw9ag8gK6eTjIvAzWoC0vBR6h57tqmMcuOCOtabZ9G84BDvIIPeo1bdcTmoPZBVgRIbang3td3a-xyzPPFe7p9fM8Qq8Gbb3s1r8_xZOrR_EU3Uz9BKJxSg_RCNTNPEPXqx8Xy3YzQQdswXzJJ2E-TryrA8rTdO5KBuV4_vF0_vUX0DBBOw
linkProvider ProQuest
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Jb9QwFLZKAcGFfQkUMBKcIKpjJ3GMhBDQVq1aRhyKNDdjxw4daeoMkw4o_Ch-I89OMtWw9NYD19hxbOd7i_02hJ5ZbSpBDI95mpM41SyJlfVufyStdGVYpvtiE3w0KsZj8XEN_RxiYbxb5cATA6M2denvyDepj8gscpazN7Ovsa8a5a2rQwmNDhb7tv0OR7bm9d4W_N_nlO5sH77fjfuqAnGZcnISC5JVNi9Ab7DcEiUUoaVS1DJSCQ4STaeF4VolDCStFlYpbQToFEaXIKw1sQzGvYAuAh_n3oWMj_nyTsdbzdJE9LE5hBWbDchHH8MGJz6f-y2LkxX5F8oE_E23_dNF8zc7bRB_O9f_t427ga71ijZ-21HGTbRm3S10uSu92d5G863BIQXXFQYtGE_bpv7RHltc1VPzCneJdRdzO7SHi64WRsOmPlYTh31kDlYOL9yiWcCnrDO1T_DisE8OaqzBusWzI2DYeNuVLL2DPp3Lgu-idVc7ex9hZvJKZJSUnKq0sJUWhsF4Nk8UyxUrI5QMqJBln5zd1wiZyuAkwArZIUnCZ2VAkkwi9GL5zqxLTXJm73cebMuePq14eFDPv8ieS8lcmKxKCqsVzVJrqSK5ISWFZRsgaAHT3BgwJnte18hTgEXo6bIZuJQ3PSln60XXpyhA2S0idK9D9nImLAOhAkpThPgK5lemutriJkchE3ooHpBlEXo5UMfptP69FQ_OXsUTdGX38MOBPNgb7T9EV2kgXhZTtoHWAXr2EbpUfjuZNPPHgfox-nzeVPMLEZ-XDQ
linkToPdf http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Jb9QwFLZKWcSFfQkUMBKcIBrHzmYkhIDpiKowmgNIvRk7duhIU2eYNKDw0_h1PDvJVMPSWw9cY8exne8t9tsQemKULjnRWZjFKQljxaJQGuf2R-JSlZolqi82kU2n-cEBn22hn0MsjHOrHHiiZ9S6Ktwd-Yi6iMw8ZSkblb1bxGw8ebX8GroKUs7SOpTT6CCyb9rvcHyrX-6N4V8_pXSy-_Htu7CvMBAWcUaOQ06S0qQ56BAmM0RySWghJTWMlDwD6abiXGdKRgykruJGSqU56BdaFSC4FTEMxj2Hzmdxkjjq-kBn6_sdZ0GLI97H6RCWj2qQlS6eDU5_Lg9cEkYbstCXDPibnvunu-ZvNlsvCidX_-dNvIau9Ao4ft1RzHW0ZewNdLErydneRKvx4KiCqxKDdowXbV39aI8MLquFfoG7hLvNygzt_gKshdGwro7k3GIXsYOlxY1t6gY-ZayuXOIXi13SUG00Vi1eHgIjx7u2YPEt9OlMFnwbbdvKmrsIM52WPKGkyKiMc1MqrhmMZ9JIslSyIkDRgBBR9EnbXe2QhfDOAywXHaoEfFZ4VIkoQM_W7yy7lCWn9n7jgLfu6dKN-wfV6ovouZdIuU7KKDdK0iQ2hkqSalJQWLYGQucwzZ0Bb6LngbU4AVuAHq-bgXs5k5S0pmq6PnkOSnAeoDsdytczYQkIG1CmApRt4H9jqpstdn7oM6T7ogJJEqDnA6WcTOvfW3Hv9FU8QpeAWMT7ven-fXSZejpmIWU7aBuQZx6gC8W343m9eugZAUafz5pofgEdX5_a
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Diversity+of+the+lysozyme+fold%3A+structure+of+the+catalytic+domain+from+an+unusual+endolysin+encoded+by+phage+Enc34&rft.jtitle=Scientific+reports&rft.au=Cernooka+Elina&rft.au=Rumnieks+Janis&rft.au=Zrelovs+Nikita&rft.au=Tars+Kaspars&rft.date=2022-03-23&rft.pub=Nature+Publishing+Group&rft.eissn=2045-2322&rft.volume=12&rft.issue=1&rft_id=info:doi/10.1038%2Fs41598-022-08765-1&rft.externalDBID=HAS_PDF_LINK
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2045-2322&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2045-2322&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2045-2322&client=summon