2luh

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'''Unreleased structure'''
 
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The entry 2luh is ON HOLD until Paper Publication
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==NMR structure of the Vta1-Vps60 complex==
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<StructureSection load='2luh' size='340' side='right'caption='[[2luh]]' 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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2LUH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2luh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2luh OCA], [https://pdbe.org/2luh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2luh RCSB], [https://www.ebi.ac.uk/pdbsum/2luh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2luh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VTA1_YEAST VTA1_YEAST] Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.<ref>PMID:12953057</ref> <ref>PMID:14701806</ref> <ref>PMID:16505166</ref> <ref>PMID:16601096</ref>
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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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Authors: Yang, Z., Vild, C., Ju, J., Zhang, X., Liu, J., Shen, J., Zhao, B., Lan, W., Gong, F., Liu, M., Cao, C., Xu, Z.
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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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Description: 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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<div class="pdbe-citations 2luh" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Cao C]]
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[[Category: Gong F]]
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[[Category: Ju J]]
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[[Category: Lan W]]
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[[Category: Liu J]]
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[[Category: Liu M]]
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[[Category: Shen J]]
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[[Category: Vild C]]
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[[Category: Xu Z]]
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[[Category: Yang Z]]
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[[Category: Zhang X]]
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[[Category: Zhao B]]

Current revision

NMR structure of the Vta1-Vps60 complex

PDB ID 2luh

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