Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution

The ESCRT-III and Vps4 complexes mediate a variety of membrane remodelling events. Here the authors describe the structure of the Vps4 hexamer complexed to its cofactor Vta1, and show that Vta1 bridges adjacent Vps4 subunits to promote formation of the active hexamer during ESCRT-III filament disass...

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Autores principales:	Shan Sun, Lin Li, Fan Yang, Xiaojing Wang, Fenghui Fan, Mengyi Yang, Chunlai Chen, Xueming Li, Hong-Wei Wang, Sen-Fang Sui
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d3659c911bdd40ed94311ab38c70deff
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spelling	oai:doaj.org-article:d3659c911bdd40ed94311ab38c70deff2021-12-02T14:42:21ZCryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution10.1038/ncomms160642041-1723https://doaj.org/article/d3659c911bdd40ed94311ab38c70deff2017-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms16064https://doaj.org/toc/2041-1723The ESCRT-III and Vps4 complexes mediate a variety of membrane remodelling events. Here the authors describe the structure of the Vps4 hexamer complexed to its cofactor Vta1, and show that Vta1 bridges adjacent Vps4 subunits to promote formation of the active hexamer during ESCRT-III filament disassembly.Shan SunLin LiFan YangXiaojing WangFenghui FanMengyi YangChunlai ChenXueming LiHong-Wei WangSen-Fang SuiNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Shan Sun Lin Li Fan Yang Xiaojing Wang Fenghui Fan Mengyi Yang Chunlai Chen Xueming Li Hong-Wei Wang Sen-Fang Sui Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
description	The ESCRT-III and Vps4 complexes mediate a variety of membrane remodelling events. Here the authors describe the structure of the Vps4 hexamer complexed to its cofactor Vta1, and show that Vta1 bridges adjacent Vps4 subunits to promote formation of the active hexamer during ESCRT-III filament disassembly.
format	article
author	Shan Sun Lin Li Fan Yang Xiaojing Wang Fenghui Fan Mengyi Yang Chunlai Chen Xueming Li Hong-Wei Wang Sen-Fang Sui
author_facet	Shan Sun Lin Li Fan Yang Xiaojing Wang Fenghui Fan Mengyi Yang Chunlai Chen Xueming Li Hong-Wei Wang Sen-Fang Sui
author_sort	Shan Sun
title	Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
title_short	Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
title_full	Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
title_fullStr	Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
title_full_unstemmed	Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
title_sort	cryo-em structures of the atp-bound vps4e233q hexamer and its complex with vta1 at near-atomic resolution
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d3659c911bdd40ed94311ab38c70deff
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Cryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution

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