3srz: Difference between revisions
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==Clostridium difficile toxin A (TcdA) glucolsyltransferase domain bound to UDP-glucose== | ==Clostridium difficile toxin A (TcdA) glucolsyltransferase domain bound to UDP-glucose== | ||
<StructureSection load='3srz' size='340' side='right' caption='[[3srz]], [[Resolution|resolution]] 2.58Å' scene=''> | <StructureSection load='3srz' size='340' side='right'caption='[[3srz]], [[Resolution|resolution]] 2.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3srz]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3srz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clod6 Clod6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SRZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ss1|3ss1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ss1|3ss1]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD0663, CD630_06630, tcdA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD0663, CD630_06630, tcdA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272563 CLOD6])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3srz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3srz OCA], [https://pdbe.org/3srz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3srz RCSB], [https://www.ebi.ac.uk/pdbsum/3srz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3srz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Clod6]] | [[Category: Clod6]] | ||
[[Category: Large Structures]] | |||
[[Category: Chumbler, N M]] | [[Category: Chumbler, N M]] | ||
[[Category: Farrow, M A]] | [[Category: Farrow, M A]] | ||
Revision as of 11:08, 29 June 2022
Clostridium difficile toxin A (TcdA) glucolsyltransferase domain bound to UDP-glucoseClostridium difficile toxin A (TcdA) glucolsyltransferase domain bound to UDP-glucose
Structural highlights
Publication Abstract from PubMedThe principle virulence factors in Clostridium difficile pathogenesis are TcdA and TcdB, homologous glucosyltransferases capable of inactivating small GTPases within the host cell. We present crystal structures of the TcdA glucosyltransferase domain (GTD) in the presence and absence of the co-substrate UDP-glucose. While the enzymatic core is similar to that of TcdB, the proposed GTPase-binding surface differs significantly. We show that TcdA is comparable to TcdB in its modification of Rho-family substrates and that, unlike TcdB, TcdA is also capable of modifying Rap-family GTPases both in vitro and in cells. The glucosyltransferase activities of both toxins are reduced in the context of the holotoxin but can be restored with autoproteolytic activation and GTD release. These studies highlight the importance of cellular activation in determining the array of substrates available to the toxins once delivered into the cell. Structural determinants of the Clostridium difficile toxin A glucosyltransferase activity.,Pruitt RN, Chumbler NM, Rutherford SA, Farrow MA, Friedman DB, Spiller B, Lacy DB J Biol Chem. 2012 Jan 20. PMID:22267739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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