1uzi
From Proteopedia
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| - | [[Image:1uzi.jpg|left|200px]]<br /><applet load="1uzi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1uzi, resolution 1.89Å" /> | ||
| - | '''C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM'''<br /> | ||
| - | == | + | ==C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM== |
| + | <StructureSection load='1uzi' size='340' side='right'caption='[[1uzi]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uzi]] is a 2 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=1UZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UZI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</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=V4O:CYCLO-TETRAMETAVANADATE'>V4O</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></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=1uzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uzi OCA], [https://pdbe.org/1uzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uzi RCSB], [https://www.ebi.ac.uk/pdbsum/1uzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uzi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARC3_CBDP ARC3_CBDP] ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uz/1uzi_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=1uzi ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and thereby inactivates Rho A, B and C GTPases in mammalian cells. The structure of a tetragonal crystal form has been determined by molecular replacement and refined to 1.89 A resolution. It is very similar to the apo structures determined previously from two different monoclinic crystal forms. An objective reassessment of available apo and nucleotide-bound C3bot1 structures indicates that, contrary to a previous report, the protein possesses a rigid core formed largely of beta-strands and that the general flexure that accompanies NAD binding is concentrated in two peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts. | C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and thereby inactivates Rho A, B and C GTPases in mammalian cells. The structure of a tetragonal crystal form has been determined by molecular replacement and refined to 1.89 A resolution. It is very similar to the apo structures determined previously from two different monoclinic crystal forms. An objective reassessment of available apo and nucleotide-bound C3bot1 structures indicates that, contrary to a previous report, the protein possesses a rigid core formed largely of beta-strands and that the general flexure that accompanies NAD binding is concentrated in two peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts. | ||
| - | + | C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure.,Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1502-5. Epub 2004, Jul 21. PMID:15272191<ref>PMID:15272191</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1uzi" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Exoenzyme 3D structures|Exoenzyme 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium botulinum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Acharya KR]] | ||
| + | [[Category: Ayriss J]] | ||
| + | [[Category: Evans HR]] | ||
| + | [[Category: Holloway DE]] | ||
| + | [[Category: Shone CC]] | ||
| + | [[Category: Sutton JM]] | ||
Current revision
C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM
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