View source for 7yvs


==Complex structure of Clostridioides difficile binary toxin unfolded CDTa-bound CDTb-pore (short).==
<StructureSection load='7yvs' size='340' side='right'caption='[[7yvs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yvs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YVS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=7yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yvs OCA], [https://pdbe.org/7yvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yvs RCSB], [https://www.ebi.ac.uk/pdbsum/7yvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yvs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8DS70_CLODI A8DS70_CLODI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Some bacteria express a binary toxin translocation system, consisting of an enzymatic subunit and translocation pore, that delivers enzymes into host cells through endocytosis. The most clinically important bacterium with such a system is Clostridioides difficile (formerly Clostridium). The CDTa and CDTb proteins from its system represent important therapeutic targets. CDTb has been proposed to be a di-heptamer, but its physiological heptameric structure has not yet been reported. Here, we report the cryo-EM structure of CDTa bound to the CDTb-pore, which reveals that CDTa binding induces partial unfolding and tilting of the first CDTa alpha-helix. In the CDTb-pore, an NSS-loop exists in 'in' and 'out' conformations, suggesting its involvement in substrate translocation. Finally, 3D variability analysis revealed CDTa movements from a folded to an unfolded state. These dynamic structural information provide insights into drug design against hypervirulent C. difficile strains.

Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.,Kawamoto A, Yamada T, Yoshida T, Sato Y, Kato T, Tsuge H Nat Commun. 2022 Oct 17;13(1):6119. doi: 10.1038/s41467-022-33888-4. PMID:36253419<ref>PMID:36253419</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yvs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridioides difficile]]
[[Category: Large Structures]]
[[Category: Kato T]]
[[Category: Kawamoto A]]
[[Category: Sato Y]]
[[Category: Tsuge H]]
[[Category: Yamada T]]
[[Category: Yoshida T]]