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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Scientific reports Jg. 12; H. 1; S. 5005 - 11
Hauptverfasser: Cernooka, Elina, Rumnieks, Janis, Zrelovs, Nikita, Tars, Kaspars, Kazaks, Andris
Format: Journal Article
Sprache:Englisch
Veröffentlicht: London Nature Publishing Group UK 23.03.2022
Nature Publishing Group
Nature Portfolio
Schlagworte:
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-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung: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.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-022-08765-1