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...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	Scientific reports Ročník 12; číslo 1; s. 5005 - 11
Hlavní autori:	Cernooka, Elina, Rumnieks, Janis, Zrelovs, Nikita, Tars, Kaspars, Kazaks, Andris
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 23.03.2022 Nature Publishing Group Nature Portfolio
Predmet:	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
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Popis
Shrnutí:	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.
Bibliografia:	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