Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
23 01 2020
23 01 2020
Historique:
received:
25
04
2019
accepted:
10
12
2019
entrez:
25
1
2020
pubmed:
25
1
2020
medline:
25
4
2020
Statut:
epublish
Résumé
Assembly of the peptidoglycan is crucial in maintaining viability of bacteria and in defining bacterial cell shapes, both of which are important for existence in the ecological niche that the organism occupies. Here, eight crystal structures for a member of the cell-shape-determining class of Campylobacter jejuni, the peptidoglycan peptidase 3 (Pgp3), are reported. Characterization of the turnover chemistry of Pgp3 reveals cell wall D,D-endopeptidase and D,D-carboxypeptidase activities. Catalysis is accompanied by large conformational changes upon peptidoglycan binding, whereby a loop regulates access to the active site. Furthermore, prior hydrolysis of the crosslinked peptide stem from the saccharide backbone of the peptidoglycan on one side is a pre-requisite for its recognition and turnover by Pgp3. These analyses reveal the noncanonical nature of the transformations at the core of the events that define the morphological shape for C. jejuni as an intestinal pathogen.
Identifiants
pubmed: 31974386
doi: 10.1038/s41467-019-13934-4
pii: 10.1038/s41467-019-13934-4
pmc: PMC6978369
doi:
Substances chimiques
Bacterial Proteins
0
Peptidoglycan
0
Virulence Factors
0
peptidoglycan endopeptidase
0
Citric Acid
2968PHW8QP
Endopeptidases
EC 3.4.-
LasA protein, Pseudomonas aeruginosa
EC 3.4.-
Metalloproteases
EC 3.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
458Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM131685
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM061629
Pays : United States
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