5b23: Difference between revisions
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==X-ray Structure of Clostridium Perfringens Sortase B== | ==X-ray Structure of Clostridium Perfringens Sortase B== | ||
<StructureSection load='5b23' size='340' side='right' caption='[[5b23]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5b23' size='340' side='right'caption='[[5b23]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5b23]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B23 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5b23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B23 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=5b23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b23 OCA], [https://pdbe.org/5b23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b23 RCSB], [https://www.ebi.ac.uk/pdbsum/5b23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b23 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8XN25_CLOPE Q8XN25_CLOPE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens str. 13]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kamitori S]] | ||
[[Category: | [[Category: Tamai E]] | ||
[[Category: | [[Category: Yoshida H]] | ||
Latest revision as of 18:56, 8 November 2023
X-ray Structure of Clostridium Perfringens Sortase BX-ray Structure of Clostridium Perfringens Sortase B
Structural highlights
FunctionPublication Abstract from PubMedThe pathogenesis and infectivity of Gram-positive bacteria are mediated by many surface proteins that are covalently attached to peptidoglycans of the cell wall. The covalent attachment of these proteins is catalyzed by sortases (Srts), a family of cysteine transpeptidases, which are classified into six classes, A - F, based on their amino acid sequences and biological roles. Clostridium perfringens, one of the pathogenic clostridial species, has a class B sortase (CpSrtB) with 249 amino acid residues. X-ray structures of CpSrtB and its inactive mutant form were determined at 2.2 A and 1.8 A resolutions, respectively. CpSrtB adopts a typical sortase-protein fold, and has a unique substrate-binding groove formed by three beta-strands and two helices creating the sidewalls of the groove. The position of the catalytic Cys232 of CpSrtB is significantly different from those commonly found in Srts structures. The modeling study of the CpSrtB/peptide complex suggested that the position of Cys232 found in CpSrtB is preferable for the catalytic reaction to occur. Structural comparison with other class B sortases demonstrated that the catalytic site likely converts between two forms. The movement of Cys232 between the two forms may help His136 deprotonate Cys232 to be activated as a thiolate, which may the catalytic Cys-activated mechanism for Srts. X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase.,Tamai E, Sekiya H, Maki J, Nariya H, Yoshida H, Kamitori S Biochem Biophys Res Commun. 2017 Nov 25;493(3):1267-1272. doi:, 10.1016/j.bbrc.2017.09.144. Epub 2017 Sep 28. PMID:28962862[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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