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Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
发布时间:2022-06-24点击次数:
影响因子: 15.0
DOI码: 10.1038/s41467-018-03785-w
发表刊物: Nat. Commun.
摘要: 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 cryo-EM at near-atomic resolutions. At least four nucleotides are bound to the AAA-ATPase ring in these open-gate states. Variation in nucleotide binding gives rise to an axial movement of the pore loops narrowing the substrate-translation channel, which exhibit remarkable structural transitions between the spiral-staircase and saddle-shaped-circle topologies. Gate opening in the CP is thus regulated by nucleotide-driven conformational changes of the AAA-ATPase unfoldase. These findings demonstrate an elegant mechanism of allosteric coordination among sub-machines within the human proteasome holoenzyme.
论文类型: 期刊论文
学科门类: 理学
文献类型: J
卷号: 9
期号: 1
页面范围: 1360
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发表时间: 2018-04-10
收录刊物: SCI
第一作者: Yanan Zhu
第一作者: Wei Li Wang
通讯作者: Ying Lu
通讯作者: Youdong Mao
合写作者: Daqi Yu
合写作者: Qi Ouyang