6jn8

Structure of H216A mutant open form peptidoglycan peptidase

spinqualitylabelsall models 6jn8, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jn8 is a 1 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.106Å Ligands: SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni.,Min K, An DR, Yoon HJ, Rana N, Park JS, Kim J, Lee M, Hesek D, Ryu S, Kim BM, Mobashery S, Suh SW, Lee HH Nat Commun. 2020 Jan 23;11(1):458. doi: 10.1038/s41467-019-13934-4. PMID:31974386 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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