This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2gza
From Proteopedia
(Difference between revisions)
| (11 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Brucella suis]] | + | <div class="pdbe-citations 2gza" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Baron | + | <references/> |
| - | [[Category: Bayliss | + | __TOC__ |
| - | [[Category: Hare | + | </StructureSection> |
| - | [[Category: Waksman | + | [[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
| |||||||||||
