2luh | pdb_00002luh
NMR structure of the Vta1-Vps60 complex
Structural highlights
FunctionVTA1_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 PubMedThe 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. See AlsoReferences
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