8yxn: Difference between revisions

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'''Unreleased structure'''


The entry 8yxn is ON HOLD
==X-ray structure of Clostridium perfringens autolysin catalytic domain in the P1 form==
<StructureSection load='8yxn' size='340' side='right'caption='[[8yxn]], [[Resolution|resolution]] 1.60&Aring;' 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]] 1.6&#8491;</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.


Authors: Kamitori, S., Tamai, E.
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>


Description: X-ray structure of Clostridium perfringens autolysin catalytic domain in the P1 form
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Tamai, E]]
<div class="pdbe-citations 8yxn" style="background-color:#fffaf0;"></div>
[[Category: Kamitori, S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Kamitori S]]
[[Category: Tamai E]]
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