Nucleotide-Driven Triple-State Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome
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ABSTRACT:
SUBMITTER: Youdong Jack Mao
PROVIDER: EMPIAR-10090 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.
Zhu Yanan Y Wang Wei Li WL Yu Daqi D Ouyang Qi Q Lu Ying Y Mao Youdong Y
Nature communications 20180410 1
The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase unfoldase in the regulatory particle (RP) control the gating of the substrate-translocation channel leading to the proteolytic chamber of the core particle (CP). Here we report three alternative states of the ATP-γ-S-bound human proteasome, in which the CP gates are asymmetrically open, visualized by c ...[more]
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