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| | <StructureSection load='2wn7' size='340' side='right'caption='[[2wn7]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='2wn7' size='340' side='right'caption='[[2wn7]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wn7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WN7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WN7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wn7]] is a 1 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=2WN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WN7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wn4|2wn4]], [[2wn5|2wn5]], [[2wn6|2wn6]], [[2wn8|2wn8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wn7 OCA], [http://pdbe.org/2wn7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wn7 RCSB], [http://www.ebi.ac.uk/pdbsum/2wn7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wn7 ProSAT]</span></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=2wn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wn7 OCA], [https://pdbe.org/2wn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2wn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wn7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KH42_CLODI Q9KH42_CLODI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus difficilis hall and o'toole 1935]] | + | [[Category: Clostridioides difficile]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Acharya KR]] |
| - | [[Category: Roberts, A K]] | + | [[Category: Roberts AK]] |
| - | [[Category: Shone, C C]] | + | [[Category: Shone CC]] |
| - | [[Category: Sundriyal, A]] | + | [[Category: Sundriyal A]] |
| - | [[Category: Actin-adprt]]
| + | |
| - | [[Category: Binary toxin]]
| + | |
| - | [[Category: Cdta]]
| + | |
| - | [[Category: Ribosyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9KH42_CLODI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
ADP-ribosylation is one of the favored modes of cell intoxication employed by several bacteria. Clostridium difficile is recognized to be an important nosocomial pathogen associated with considerable morbidity and attributable mortality. Along with its two well known toxins, Toxin A and Toxin B, it produces an ADP-ribosylating toxin that targets monomeric actin of the target cell. Like other Clostridial actin ADP-ribosylating toxins, this binary toxin, known as C. difficile toxin (CDT), is composed of two subunits, CDTa and CDTb. In this study, we present high resolution crystal structures of CDTa in its native form (at pH 4.0, 8.5, and 9.0) and in complex with ADP-ribose donors, NAD and NADPH (at pH 9.0). The crystal structures of the native protein show "pronounced conformational flexibility" confined to the active site region of the protein and "enhanced" disorder at low pH, whereas the complex structures highlight significant differences in "ligand specificity" compared with the enzymatic subunit of a close homologue, Clostridium perfringens iota toxin. Specifically in CDTa, two of the suggested catalytically important residues (Glu-385 and Glu-387) seem to play no role or a less important role in ligand binding. These structural data provide the first detailed information on protein-donor substrate complex stabilization in CDTa, which may have implications in understanding CDT recognition.
Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from Clostridium difficile.,Sundriyal A, Roberts AK, Shone CC, Acharya KR J Biol Chem. 2009 Oct 16;284(42):28713-9. Epub 2009 Aug 19. PMID:19692332[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sundriyal A, Roberts AK, Shone CC, Acharya KR. Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from Clostridium difficile. J Biol Chem. 2009 Oct 16;284(42):28713-9. Epub 2009 Aug 19. PMID:19692332 doi:10.1074/jbc.M109.043018
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