6JMY

Structure of wild type closed form of peptidoglycan peptidase

Summary for 6JMY

• Entry DOI: 10.2210/pdb6jmy/pdb
• Descriptor: Peptidase M23, ZINC ION, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: peptidoglycan, hydrolase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 1
• Total formula weight: 29746.34

Authors

Min, K.J.,An, D.R.,Yoon, H.J.,Suh, S.W.,Lee, H.H. (deposition date: 2019-03-13, release date: 2020-01-15, Last modification date: 2024-05-29)

Primary citation

Min, K.,An, D.R.,Yoon, H.J.,Rana, N.,Park, J.S.,Kim, J.,Lee, M.,Hesek, D.,Ryu, S.,Kim, B.M.,Mobashery, S.,Suh, S.W.,Lee, H.H.
Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni.
Nat Commun, 11:458-458, 2020

PubMed Abstract: 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.

PubMed: 31974386
DOI: 10.1038/s41467-019-13934-4

Experimental method

X-RAY DIFFRACTION (1.661 Å)