2c8d

From Proteopedia

(Difference between revisions)

Revision as of 23:58, 11 September 2015

STRUCTURE OF THE ARTT MOTIF Q212A MUTANT C3BOT1 EXOENZYME (FREE STATE, CRYSTAL FORM I)

Structural highlights

2c8d is a 4 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1g24, 1gze, 1gzf, 1uzi, 2a78, 2a9k, 2bov, 2c89, 2c8a, 2c8b, 2c8c, 2c8e, 2c8f, 2c8g, 2c8h
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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 PubMed

C3-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.

References

↑ Menetrey J, Flatau G, Boquet P, Menez A, Stura EA. Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes. Protein Sci. 2008 May;17(5):878-86. Epub 2008 Mar 27. PMID:18369192 doi:10.1110/ps.073398508

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c8d"

@@ Line 2: / Line 2: @@
 <StructureSection load='2c8d' size='340' side='right' caption='[[2c8d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c8d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C8D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c8d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C8D FirstGlance]. <br>
 </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]], [[1gzf|1gzf]], [[1uzi|1uzi]], [[2a78|2a78]], [[2a9k|2a9k]], [[2bov|2bov]], [[2c89|2c89]], [[2c8a|2c8a]], [[2c8b|2c8b]], [[2c8c|2c8c]], [[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=2c8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c8d RCSB], [http://www.ebi.ac.uk/pdbsum/2c8d 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=2c8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8d OCA], [http://pdbe.org/2c8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c8d RCSB], [http://www.ebi.ac.uk/pdbsum/2c8d PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c8d" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Clostridium botulinum]]
+[[Category: Bacillus botulinus van ermengem 1896]]
 [[Category: Boquet, P]]
 [[Category: Flatau, G]]

2c8d

From Proteopedia

Revision as of 23:58, 11 September 2015

STRUCTURE OF THE ARTT MOTIF Q212A MUTANT C3BOT1 EXOENZYME (FREE STATE, CRYSTAL FORM I)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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