6UTF

Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome singly capped with a PAN complex

6UTF の概要

• エントリーDOI: 10.2210/pdb6utf/pdb
• EMDBエントリー: 20877 20878 20879 20880 20881
• 分子名称: Proteasome subunit beta, Proteasome subunit alpha (3 entities in total)
• 機能のキーワード: proteasome, pan, singly-capped, hydrolase
• 由来する生物種: Thermoplasma acidophilum; 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 675421.07

構造登録者

Cheng, Y.,Yu, Z. (登録日: 2019-10-29, 公開日: 2020-09-09, 最終更新日: 2025-06-04)

主引用文献

Yu, Z.,Yu, Y.,Wang, F.,Myasnikov, A.G.,Coffino, P.,Cheng, Y.
Allosteric coupling between alpha-rings of the 20S proteasome.
Nat Commun, 11:4580-4580, 2020

PubMed Abstract: Proteasomal machinery performs essential regulated protein degradation in eukaryotes. Classic proteasomes are symmetric, with a regulatory ATPase docked at each end of the cylindrical 20S. Asymmetric complexes are also present in cells, either with a single ATPase or with an ATPase and non-ATPase at two opposite ends. The mechanism that populates these different proteasomal complexes is unknown. Using archaea homologs, we construct asymmetric forms of proteasomes. We demonstrate that the gate conformation of the two opposite ends of 20S are coupled: binding one ATPase opens a gate locally, and also opens the opposite gate allosterically. Such allosteric coupling leads to cooperative binding of proteasomal ATPases to 20S and promotes formation of proteasomes symmetrically configured with two identical ATPases. It may also promote formation of asymmetric complexes with an ATPase and a non-ATPase at opposite ends. We propose that in eukaryotes a similar mechanism regulates the composition of the proteasomal population.

PubMed: 32917864
DOI: 10.1038/s41467-020-18415-7

実験手法

ELECTRON MICROSCOPY (3.4 Å)