5T0C

Structural basis for dynamic regulation of the human 26S proteasome

これはPDB形式変換不可エントリーです。

5T0C の概要

• エントリーDOI: 10.2210/pdb5t0c/pdb
• 関連するPDBエントリー: 5T0G 5T0H 5T0I 5T0J
• EMDBエントリー: 8332 8333 8334 8335 8336 8337
• 分子名称: 26S proteasome non-ATPase regulatory subunit 1, 26S proteasome non-ATPase regulatory subunit 8, 26S proteasome complex subunit DSS1, ... (35 entities in total)
• 機能のキーワード: ubiquitin-proteasome system, aaa-atpase, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 64
• 化学式量合計: 2548853.32

構造登録者

Chen, S.,Wu, J.,Lu, Y.,Ma, Y.B.,Lee, B.H.,Yu, Z.,Ouyang, Q.,Finley, D.,Kirschner, M.W.,Mao, Y. (登録日: 2016-08-15, 公開日: 2016-10-19, 最終更新日: 2024-11-06)

主引用文献

Chen, S.,Wu, J.,Lu, Y.,Ma, Y.B.,Lee, B.H.,Yu, Z.,Ouyang, Q.,Finley, D.J.,Kirschner, M.W.,Mao, Y.
Structural basis for dynamic regulation of the human 26S proteasome.
Proc.Natl.Acad.Sci.USA, 113:12991-12996, 2016

PubMed Abstract: The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitylated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Using cryoelectron microscopy, we determined a near-atomic-resolution structure of the 2.5-MDa human proteasome in its ground state, as well as subnanometer-resolution structures of the holoenzyme in three alternative conformational states. The substrate-unfolding AAA-ATPase channel is narrowed by 10 inward-facing pore loops arranged into two helices that run in parallel with each other, one hydrophobic in character and the other highly charged. The gate of the core particle was unexpectedly found closed in the ground state and open in only one of the alternative states. Coordinated, stepwise conformational changes of the regulatory particle couple ATP hydrolysis to substrate translocation and regulate gating of the core particle, leading to processive degradation.

PubMed: 27791164
DOI: 10.1073/pnas.1614614113

実験手法

ELECTRON MICROSCOPY (3.8 Å)