5MPD

26S proteasome in presence of ATP (s1)

5MPD の概要

• エントリーDOI: 10.2210/pdb5mpd/pdb
• EMDBエントリー: 3534
• 分子名称: 26S proteasome regulatory subunit RPN10, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit RPN7, ... (13 entities in total)
• 機能のキーワード: macromolecular complex, 26s proteasome, protease, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm : O13563
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 633806.38

構造登録者

Wehmer, M.,Rudack, T.,Beck, F.,Aufderheide, A.,Pfeifer, G.,Plitzko, J.M.,Foerster, F.,Schulten, K.,Baumeister, W.,Sakata, E. (登録日: 2016-12-16, 公開日: 2017-03-08, 最終更新日: 2024-05-08)

主引用文献

Wehmer, M.,Rudack, T.,Beck, F.,Aufderheide, A.,Pfeifer, G.,Plitzko, J.M.,Forster, F.,Schulten, K.,Baumeister, W.,Sakata, E.
Structural insights into the functional cycle of the ATPase module of the 26S proteasome.
Proc. Natl. Acad. Sci. U.S.A., 114:1305-1310, 2017

PubMed Abstract: In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for the regulated degradation of intracellular proteins. The 26S holocomplex comprises the core particle (CP), where proteolysis takes place, and one or two regulatory particles (RPs). The base of the RP is formed by a heterohexameric AAA ATPase module, which unfolds and translocates substrates into the CP. Applying single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states (s1 to s4). The resolution of the four conformers allowed for the construction of atomic models of the AAA ATPase module as it progresses through the functional cycle. In a hitherto unobserved state (s4), the gate controlling access to the CP is open. The structures described in this study allow us to put forward a model for the 26S functional cycle driven by ATP hydrolysis.

PubMed: 28115689
DOI: 10.1073/pnas.1621129114

実験手法

ELECTRON MICROSCOPY (4.1 Å)