2luh

From Proteopedia

(Difference between revisions)

Revision as of 00:27, 25 December 2014

NMR structure of the Vta1-Vps60 complex

Structural highlights

2luh is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	VTA1, YLR181C (Saccharomyces cerevisiae S288c), VPS60, CHM5, MOS10, YDR486C (Saccharomyces cerevisiae S288c)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yeo SC, Xu L, Ren J, Boulton VJ, Wagle MD, Liu C, Ren G, Wong P, Zahn R, Sasajala P, Yang H, Piper RC, Munn AL. Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae. J Cell Sci. 2003 Oct 1;116(Pt 19):3957-70. PMID:12953057 doi:http://dx.doi.org/10.1242/jcs.00751
↑ Shiflett SL, Ward DM, Huynh D, Vaughn MB, Simmons JC, Kaplan J. Characterization of Vta1p, a class E Vps protein in Saccharomyces cerevisiae. J Biol Chem. 2004 Mar 19;279(12):10982-90. Epub 2003 Dec 29. PMID:14701806 doi:10.1074/jbc.M312669200
↑ Azmi I, Davies B, Dimaano C, Payne J, Eckert D, Babst M, Katzmann DJ. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J Cell Biol. 2006 Feb 27;172(5):705-17. PMID:16505166 doi:jcb.200508166
↑ Lottridge JM, Flannery AR, Vincelli JL, Stevens TH. Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body. Proc Natl Acad Sci U S A. 2006 Apr 18;103(16):6202-7. Epub 2006 Apr 6. PMID:16601096 doi:0601712103
↑ Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. Structural basis of molecular recognition between ESCRT-III like protein Vps60 and AAA-ATPase regulator Vta1 in the multi-vesicular body pathway. J Biol Chem. 2012 Oct 26. PMID:23105107 doi:http://dx.doi.org/10.1074/jbc.M112.390724

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2luh"

@@ Line 6: / Line 6: @@
 <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>
 </table>
+== Function ==
+[[http://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 21: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae s288c]]
-[[Category: Cao, C.]]
+[[Category: Cao, C]]
-[[Category: Gong, F.]]
+[[Category: Gong, F]]
-[[Category: Ju, J.]]
+[[Category: Ju, J]]
-[[Category: Lan, W.]]
+[[Category: Lan, W]]
-[[Category: Liu, J.]]
+[[Category: Liu, J]]
-[[Category: Liu, M.]]
+[[Category: Liu, M]]
-[[Category: Shen, J.]]
+[[Category: Shen, J]]
-[[Category: Vild, C.]]
+[[Category: Vild, C]]
-[[Category: Xu, Z.]]
+[[Category: Xu, Z]]
-[[Category: Yang, Z.]]
+[[Category: Yang, Z]]
-[[Category: Zhang, X.]]
+[[Category: Zhang, X]]
-[[Category: Zhao, B.]]
+[[Category: Zhao, B]]
 [[Category: Endocytosis]]
 [[Category: Escrt]]

2luh

From Proteopedia

Revision as of 00:27, 25 December 2014

NMR structure of the Vta1-Vps60 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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