View source for 3zrj


==Complex of ClpV N-domain with VipB peptide==
<StructureSection load='3zrj' size='340' side='right'caption='[[3zrj]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zrj]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3ZRJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[3zri|3zri]]</div></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=3zrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zrj OCA], [https://pdbe.org/3zrj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zrj RCSB], [https://www.ebi.ac.uk/pdbsum/3zrj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zrj ProSAT]</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zrj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae v52]]
[[Category: Kopp, J]]
[[Category: Lenherr, E D]]
[[Category: Sinning, I]]
[[Category: Aaa+ protein]]
[[Category: Chaperone-peptide complex]]
[[Category: Hsp100 protein]]
[[Category: Secretion]]
[[Category: T6ss]]
[[Category: Virulence]]