<table><tr><td colspan='2'>[[5xmk]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XMK FirstGlance]. <br>
<table><tr><td colspan='2'>[[5xmk]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XMK FirstGlance]. <br>
5xmk is a 14 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[VPS4_YEAST] Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.[1][2][3] [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.[4][5][6][7]
Publication Abstract from PubMed
The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is essential for the machinery function by using the energy from ATP hydrolysis to disassemble the ESCRT-III polymer into individual proteins. Here, we report the structures of the ATP-bound Vps4E233Q hexamer and its complex with the cofactor Vta1 (vps twenty associated 1) at resolutions of 3.9 and 4.2 A, respectively, determined by electron cryo-microscopy. Six Vps4E233Q subunits in both assemblies exhibit a spiral-shaped ring-like arrangement. Locating at the periphery of the hexameric ring, Vta1 dimer bridges two adjacent Vps4 subunits by two different interaction modes to promote the formation of the active Vps4 hexamer during ESCRT-III filament disassembly. The structural findings, together with the structure-guided biochemical and single-molecule analyses, provide important insights into the process of the ESCRT-III polymer disassembly by Vps4.
Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution.,Sun S, Li L, Yang F, Wang X, Fan F, Yang M, Chen C, Li X, Wang HW, Sui SF Nat Commun. 2017 Jul 17;8:16064. doi: 10.1038/ncomms16064. PMID:28714467[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Zahn R, Stevenson BJ, Schroder-Kohne S, Zanolari B, Riezman H, Munn AL. End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae. J Cell Sci. 2001 May;114(Pt 10):1935-47. PMID:11329380
↑ Babst M, Sato TK, Banta LM, Emr SD. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 1997 Apr 15;16(8):1820-31. PMID:9155008 doi:10.1093/emboj/16.8.1820
↑ Babst M, Wendland B, Estepa EJ, Emr SD. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 1998 Jun 1;17(11):2982-93. PMID:9606181 doi:10.1093/emboj/17.11.2982
↑ 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
↑ Sun S, Li L, Yang F, Wang X, Fan F, Yang M, Chen C, Li X, Wang HW, Sui SF. Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution. Nat Commun. 2017 Jul 17;8:16064. doi: 10.1038/ncomms16064. PMID:28714467 doi:http://dx.doi.org/10.1038/ncomms16064
