8yxn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of Clostridium perfringens autolysin catalytic domain in the P1 form== | |
| + | <StructureSection load='8yxn' size='340' side='right'caption='[[8yxn]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8yxn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YXN 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]] 1.6Å</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=8yxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yxn OCA], [https://pdbe.org/8yxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yxn RCSB], [https://www.ebi.ac.uk/pdbsum/8yxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yxn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2Z3TZM8_CLOPF A0A2Z3TZM8_CLOPF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clostridioides difficile endolysin (Ecd09610) consists of an unknown domain at its N terminus, followed by two catalytic domains, a glucosaminidase domain and endopeptidase domain. X-ray structure and mutagenesis analyses of the Ecd09610 catalytic domain with glucosaminidase activity (Ecd09610CD53) were performed. Ecd09610CD53 was found to possess an alpha-bundle-like structure with nine helices, which is well conserved among GH73 family enzymes. The mutagenesis analysis based on X-ray structures showed that Glu405 and Asn470 were essential for enzymatic activity. Ecd09610CD53 may adopt a neighboring-group mechanism for a catalytic reaction in which Glu405 acted as an acid/base catalyst and Asn470 helped to stabilize the oxazolinium ion intermediate. Structural comparisons with the newly identified Clostridium perfringens autolysin catalytic domain (AcpCD) in the P1 form and a zymography analysis demonstrated that AcpCD was 15-fold more active than Ecd09610CD53. The strength of the glucosaminidase activity of the GH73 family appears to be dependent on the depth of the substrate-binding groove. | ||
| - | + | X-ray structure and mutagenesis analyses of Clostridioides difficile endolysin Ecd09610 glucosaminidase domain.,Sekiya H, Nonaka Y, Kamitori S, Miyaji T, Tamai E Biochem Biophys Res Commun. 2024 Jun 30;715:149957. doi: , 10.1016/j.bbrc.2024.149957. Epub 2024 Apr 16. PMID:38688057<ref>PMID:38688057</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8yxn" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kamitori | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium perfringens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kamitori S]] | ||
| + | [[Category: Tamai E]] | ||
Current revision
X-ray structure of Clostridium perfringens autolysin catalytic domain in the P1 form
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