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==STRUCTURE OF THE PN LOOP Q182A MUTANT C3BOT1 EXOENZYME (NAD-BOUND STATE, CRYSTAL FORM I)==
 
<StructureSection load='2c8h' size='340' side='right' caption='[[2c8h]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
==Structure of the PN loop Q182A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)==
<StructureSection load='2c8h' size='340' side='right'caption='[[2c8h]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c8h]] 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=2C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C8H FirstGlance]. <br>
<table><tr><td colspan='2'>[[2c8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C8H FirstGlance]. <br>
</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.65&#8491;</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]], [[2c8d|2c8d]], [[2c8e|2c8e]], [[2c8f|2c8f]], [[2c8g|2c8g]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c8h RCSB], [http://www.ebi.ac.uk/pdbsum/2c8h PDBsum]</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=2c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8h OCA], [https://pdbe.org/2c8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c8h RCSB], [https://www.ebi.ac.uk/pdbsum/2c8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c8h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ARC3_CBDP ARC3_CBDP]] ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.
[https://www.uniprot.org/uniprot/Q7M0L1_CLOBO Q7M0L1_CLOBO]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c8h_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/2c8h_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=2c8h ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have solved the crystal structures of Clostridium botulinum C3 exoenzyme free and complexed to NAD in the same crystal form, at 2.7 and 1.95 A, respectively. The asymmetric unit contains four molecules, which, in the free form, share the same conformation. Upon NAD binding, C3 underwent various conformational changes, whose amplitudes were differentially limited in the four molecules of the crystal unit. A major rearrangement concerns the loop that contains the functionally important ARTT motif (ADP-ribosyltransferase toxin turn-turn). The ARTT loop undergoes an ample swinging motion to adopt a conformation that covers the nicotinamide moiety of NAD. In particular, Gln-212, which belongs to the ARTT motif, flips over from a solvent-exposed environment to a buried conformation in the NAD binding pocket. Mutational experiments showed that Gln-212 is neither involved in NAD binding nor in the NAD-glycohydrolase activity of C3, whereas it plays a critical role in the ADP-ribosyl transfer to the substrate Rho. We observed additional NAD-induced movements, including a crab-claw motion of a subdomain that closes the NAD binding pocket. The data emphasized a remarkable NAD-induced plasticity of the C3 binding pocket and suggest that the NAD-induced ARTT loop conformation may be favored by the C3-NAD complex to bind to the substrate Rho. Our structural observations, together with a number of mutational experiments suggest that the mechanisms of Rho ADP-ribosylation by C3-NAD may be more complex than initially anticipated.
NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme.,Menetrey J, Flatau G, Stura EA, Charbonnier JB, Gas F, Teulon JM, Le Du MH, Boquet P, Menez A J Biol Chem. 2002 Aug 23;277(34):30950-7. Epub 2002 May 23. PMID:12029083<ref>PMID:12029083</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Exoenzyme|Exoenzyme]]
*[[Exoenzyme 3D structures|Exoenzyme 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Boquet, P]]
[[Category: Large Structures]]
[[Category: Flatau, G]]
[[Category: Boquet P]]
[[Category: Menetrey, J]]
[[Category: Flatau G]]
[[Category: Menez, A]]
[[Category: Menetrey J]]
[[Category: Stura, E A]]
[[Category: Menez A]]
[[Category: Adp-ribosyltransferase]]
[[Category: Stura EA]]
[[Category: Artt motif]]
[[Category: Bacterial toxin]]
[[Category: C3 exoenzyme]]
[[Category: Glycosyltransferase]]
[[Category: Nad]]
[[Category: Pn loop]]
[[Category: Transferase]]

Latest revision as of 17:09, 13 December 2023

Structure of the PN loop Q182A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)Structure of the PN loop Q182A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)

Structural highlights

2c8h is a 4 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7M0L1_CLOBO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2c8h, resolution 1.65Å

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OCA
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