2c89: Difference between revisions
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==Structure of the wild-type C3bot1 Exoenzyme (Free state, crystal form I)== | |||
<StructureSection load='2c89' size='340' side='right' caption='[[2c89]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2c89' size='340' side='right' caption='[[2c89]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g24|1g24]], [[1gze|1gze]], [[1uzi|1uzi]], [[1gzf|1gzf]], [[2a78|2a78]], [[2a9k|2a9k]], [[2bov|2bov]], [[2c8a|2c8a]], [[2c8b|2c8b]], [[2c8c|2c8c]], [[2c8d|2c8d]], [[2c8e|2c8e]], [[2c8f|2c8f]], [[2c8g|2c8g]], [[2c8h|2c8h]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g24|1g24]], [[1gze|1gze]], [[1uzi|1uzi]], [[1gzf|1gzf]], [[2a78|2a78]], [[2a9k|2a9k]], [[2bov|2bov]], [[2c8a|2c8a]], [[2c8b|2c8b]], [[2c8c|2c8c]], [[2c8d|2c8d]], [[2c8e|2c8e]], [[2c8f|2c8f]], [[2c8g|2c8g]], [[2c8h|2c8h]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c89 OCA], [http://pdbe.org/2c89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c89 RCSB], [http://www.ebi.ac.uk/pdbsum/2c89 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c89 OCA], [http://pdbe.org/2c89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c89 RCSB], [http://www.ebi.ac.uk/pdbsum/2c89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c89 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c89_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c89_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:59, 23 May 2018
Structure of the wild-type C3bot1 Exoenzyme (Free state, crystal form I)Structure of the wild-type C3bot1 Exoenzyme (Free state, crystal form I)
Structural highlights
Function[ARC3_CBDP] ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. 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 PubMedC3-like exoenzymes are ADP-ribosyltransferases that specifically modify some Rho GTPase proteins, leading to their sequestration in the cytoplasm, and thus inhibiting their regulatory activity on the actin cytoskeleton. This modification process goes through three sequential steps involving NAD-hydrolysis, Rho recognition, and binding, leading to Rho ADP-ribosylation. Independently, three distinct residues within the ARTT loop of the C3 exoenzymes are critical for each of these steps. Supporting the critical role of the ARTT loop, we have shown previously that it adopts a distinct conformation upon NAD binding. Here, we present seven wild-type and ARTT loop-mutant structures of C3 exoenzyme of Clostridium botulinum free and bound to its true substrate, NAD, and to its NAD-hydrolysis product, nicotinamide. Altogether, these structures expand our understanding of the conformational diversity of the C3 exoenzyme, mainly within the ARTT loop. Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes.,Menetrey J, Flatau G, Boquet P, Menez A, Stura EA Protein Sci. 2008 May;17(5):878-86. Epub 2008 Mar 27. PMID:18369192[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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