2luh

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[[Image:2luh.png|left|200px]]
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==NMR structure of the Vta1-Vps60 complex==
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<StructureSection load='2luh' size='340' side='right' caption='[[2luh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2luh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LUH FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VTA1, YLR181C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), VPS60, CHM5, MOS10, YDR486C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
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<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=2luh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2luh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2luh RCSB], [http://www.ebi.ac.uk/pdbsum/2luh PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The AAA-ATPase Vps4 is critical for function of multivesicular bodies (MVB) sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear. The fragment Vps60 (128-186aa) was reported to display full activity of Vps60. Vta1 interacts with Vps60 by using its N-terminus (named as Vta1NTD). In this paper, the structure of Vps60(128-186aa) in complex with N-terminal Vta1 was determined by using NMR techniques, demonstrating a novel recognition mode of microtubule-interacting and transport (MIT) domain, in which Vps60(128-186aa) interacts with Vta1NTD through its helices 4 and 5 extending over Vta1NTD MIT2 domain helices 1, 2 and 3. The Vps60 binding does not result in Vta1 conformational changes, further revealing the fact that Vps4 ATPase is enhanced by the interaction between Vta1 and Vps60 in an unanticipated manner.
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{{STRUCTURE_2luh| PDB=2luh | SCENE= }}
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Structural basis of molecular recognition between ESCRT-III like protein Vps60 and AAA-ATPase regulator Vta1 in the multi-vesicular body pathway.,Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z J Biol Chem. 2012 Oct 26. PMID:23105107<ref>PMID:23105107</ref>
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===NMR structure of the Vta1-Vps60 complex===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_23105107}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2luh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LUH OCA].
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</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Cao, C.]]
[[Category: Cao, C.]]

Revision as of 11:35, 20 October 2014

NMR structure of the Vta1-Vps60 complex

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