Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides mechanistic insights into gate opening and dynamic r...

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Autores principales:	Yanan Zhu, Wei Li Wang, Daqi Yu, Qi Ouyang, Ying Lu, Youdong Mao
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/db4b804dc56b4cd2bb2a2dc1b71eeb2d
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spelling	oai:doaj.org-article:db4b804dc56b4cd2bb2a2dc1b71eeb2d2021-12-02T17:33:17ZStructural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome10.1038/s41467-018-03785-w2041-1723https://doaj.org/article/db4b804dc56b4cd2bb2a2dc1b71eeb2d2018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03785-whttps://doaj.org/toc/2041-1723The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides mechanistic insights into gate opening and dynamic remodeling of the substrate–translocation pathway.Yanan ZhuWei Li WangDaqi YuQi OuyangYing LuYoudong MaoNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yanan Zhu Wei Li Wang Daqi Yu Qi Ouyang Ying Lu Youdong Mao Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
description	The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides mechanistic insights into gate opening and dynamic remodeling of the substrate–translocation pathway.
format	article
author	Yanan Zhu Wei Li Wang Daqi Yu Qi Ouyang Ying Lu Youdong Mao
author_facet	Yanan Zhu Wei Li Wang Daqi Yu Qi Ouyang Ying Lu Youdong Mao
author_sort	Yanan Zhu
title	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
title_short	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
title_full	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
title_fullStr	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
title_full_unstemmed	Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
title_sort	structural mechanism for nucleotide-driven remodeling of the aaa-atpase unfoldase in the activated human 26s proteasome
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/db4b804dc56b4cd2bb2a2dc1b71eeb2d
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Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

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