6JMY

Structure of wild type closed form of peptidoglycan peptidase

6JMY の概要

• エントリーDOI: 10.2210/pdb6jmy/pdb
• 分子名称: Peptidase M23, ZINC ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: peptidoglycan, hydrolase
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29746.34

構造登録者

Min, K.J.,An, D.R.,Yoon, H.J.,Suh, S.W.,Lee, H.H. (登録日: 2019-03-13, 公開日: 2020-01-15, 最終更新日: 2024-05-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.661 Å)