3zrj
From Proteopedia
(Difference between revisions)
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| - | + | ==Complex of ClpV N-domain with VipB peptide== | |
| - | === | + | <StructureSection load='3zrj' size='340' side='right' caption='[[3zrj]], [[Resolution|resolution]] 1.94Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3zrj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae_v52 Vibrio cholerae v52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZRJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZRJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zri|3zri]]</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=3zrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zrj RCSB], [http://www.ebi.ac.uk/pdbsum/3zrj PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ring-forming AAA(+) ATPases act in a plethora of cellular processes by remodeling macromolecules. The specificity of individual AAA(+) proteins is achieved by direct or adaptor-mediated association with substrates via distinct recognition domains. We investigated the molecular basis of substrate interaction for Vibrio cholerae ClpV, which disassembles tubular VipA/VipB complexes, an essential step of type VI protein secretion and bacterial virulence. We identified the ClpV recognition site within VipB, showed that productive ClpV-VipB interaction requires the oligomeric state of both proteins, solved the crystal structure of a ClpV N-domain-VipB peptide complex, and verified the interaction surface by mutant analysis. Our results show that the substrate is bound to a hydrophobic groove, which is formed by the addition of a single alpha-helix to the core N-domain. This helix is absent from homologous N-domains, explaining the unique substrate specificity of ClpV. A limited interaction surface between both proteins accounts for the dramatic increase in binding affinity upon ATP-driven ClpV hexamerization and VipA/VipB tubule assembly by coupling multiple weak interactions. This principle ensures ClpV selectivity toward the VipA/VipB macromolecular complex. | ||
| - | + | Molecular basis for the unique role of the AAA+ chaperone ClpV in type VI protein secretion.,Pietrosiuk A, Lenherr ED, Falk S, Bonemann G, Kopp J, Zentgraf H, Sinning I, Mogk A J Biol Chem. 2011 Aug 26;286(34):30010-21. doi: 10.1074/jbc.M111.253377. Epub, 2011 Jul 5. PMID:21733841<ref>PMID:21733841</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Vibrio cholerae v52]] | [[Category: Vibrio cholerae v52]] | ||
| - | [[Category: Kopp, J | + | [[Category: Kopp, J]] |
| - | [[Category: Lenherr, E D | + | [[Category: Lenherr, E D]] |
| - | [[Category: Sinning, I | + | [[Category: Sinning, I]] |
[[Category: Aaa+ protein]] | [[Category: Aaa+ protein]] | ||
[[Category: Chaperone-peptide complex]] | [[Category: Chaperone-peptide complex]] | ||
Revision as of 08:23, 15 February 2015
Complex of ClpV N-domain with VipB peptide
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