2c8f: Difference between revisions

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==STRUCTURE OF THE ARTT MOTIF E214N MUTANT C3BOT1 EXOENZYME (NAD-BOUND STATE, CRYSTAL FORM III)==
 
==Structure of the ARTT motif E214N mutant C3bot1 Exoenzyme (NAD-bound state, crystal form III)==
<StructureSection load='2c8f' size='340' side='right' caption='[[2c8f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2c8f' size='340' side='right' caption='[[2c8f]], [[Resolution|resolution]] 2.50&Aring;' 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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]], [[2c8a|2c8a]], [[2c8b|2c8b]], [[2c8c|2c8c]], [[2c8d|2c8d]], [[2c89|2c89]], [[2c8e|2c8e]], [[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]], [[2c8a|2c8a]], [[2c8b|2c8b]], [[2c8c|2c8c]], [[2c8d|2c8d]], [[2c89|2c89]], [[2c8e|2c8e]], [[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=2c8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8f OCA], [http://pdbe.org/2c8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c8f RCSB], [http://www.ebi.ac.uk/pdbsum/2c8f 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=2c8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8f OCA], [http://pdbe.org/2c8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c8f RCSB], [http://www.ebi.ac.uk/pdbsum/2c8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c8f 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/c8/2c8f_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c8f_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>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c8f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 11:38, 23 May 2018

Structure of the ARTT motif E214N mutant C3bot1 Exoenzyme (NAD-bound state, crystal form III)Structure of the ARTT motif E214N mutant C3bot1 Exoenzyme (NAD-bound state, crystal form III)

Structural highlights

2c8f is a 3 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:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. 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

2c8f, resolution 2.50Å

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OCA