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

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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Main Authors: Yanan Zhu, Wei Li Wang, Daqi Yu, Qi Ouyang, Ying Lu, Youdong Mao
Format: Article
Language:English
Published: Nature Publishing Group 2018-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-03785-w
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spelling doaj-db4b804dc56b4cd2bb2a2dc1b71eeb2d2021-05-11T10:10:52ZengNature Publishing GroupNature Communications2041-17232018-04-019111210.1038/s41467-018-03785-wStructural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasomeYanan Zhu0Wei Li Wang1Daqi Yu2Qi Ouyang3Ying Lu4Youdong Mao5Center for Quantitative Biology, Peking UniversityIntel Parallel Computing Center for Structural Biology, Dana-Farber Cancer InstituteState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter and Material Physics, School of Physics, Peking UniversityCenter for Quantitative Biology, Peking UniversityDepartment of Systems Biology, Harvard Medical SchoolCenter for Quantitative Biology, Peking UniversityThe 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.https://doi.org/10.1038/s41467-018-03785-w
collection DOAJ
language English
format Article
sources DOAJ
author Yanan Zhu
Wei Li Wang
Daqi Yu
Qi Ouyang
Ying Lu
Youdong Mao
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-04-01
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.
url https://doi.org/10.1038/s41467-018-03785-w
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