6jmx: Difference between revisions
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==Structure of open form of peptidoglycan peptidase== | |||
<StructureSection load='6jmx' size='340' side='right'caption='[[6jmx]], [[Resolution|resolution]] 1.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jmx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JMX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.859Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jmx OCA], [https://pdbe.org/6jmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jmx RCSB], [https://www.ebi.ac.uk/pdbsum/6jmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jmx ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:31974386</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6jmx" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Campylobacter jejuni]] | |||
[[Category: Large Structures]] | |||
[[Category: An DR]] | |||
[[Category: Lee HH]] | |||
[[Category: Min KJ]] | |||
[[Category: Suh SW]] | |||
[[Category: Yoon HJ]] | |||
Latest revision as of 22:27, 29 May 2024
Structure of open form of peptidoglycan peptidaseStructure of open form of peptidoglycan peptidase
Structural highlights
Publication Abstract from PubMedAssembly 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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