2gza
From Proteopedia
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| - | [[Image:2gza.gif|left|200px]] | ||
| - | + | ==Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate== | |
| - | + | <StructureSection load='2gza' size='340' side='right'caption='[[2gza]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2gza]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_suis_1330 Brucella suis 1330]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZA 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]] 2.6Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=2gza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gza OCA], [https://pdbe.org/2gza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gza RCSB], [https://www.ebi.ac.uk/pdbsum/2gza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gza ProSAT]</span></td></tr> | |
| - | | | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/VIRBB_BRUSU VIRBB_BRUSU] The VirB system could be required for the establishment of the replication niche in the host. | |
| - | + | == 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/gz/2gza_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=2gza ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits. | VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits. | ||
| - | + | A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact.,Hare S, Bayliss R, Baron C, Waksman G J Mol Biol. 2006 Jun 30;360(1):56-66. Epub 2006 May 11. PMID:16730027<ref>PMID:16730027</ref> | |
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| - | A large domain swap in the VirB11 ATPase of Brucella suis leaves the hexameric assembly intact., Hare S, Bayliss R, Baron C, Waksman G | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2gza" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brucella suis 1330]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baron C]] | ||
| + | [[Category: Bayliss R]] | ||
| + | [[Category: Hare S]] | ||
| + | [[Category: Waksman G]] | ||
Current revision
Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate
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