7LS5

Cryo-EM structure of the Pre3-1 20S proteasome core particle

7LS5 の概要

• エントリーDOI: 10.2210/pdb7ls5/pdb
• EMDBエントリー: 23502
• 分子名称: Proteasome subunit alpha type-1, Proteasome subunit beta type-3, Proteasome subunit beta type-4, ... (14 entities in total)
• 機能のキーワード: core particle, complex, assembly intermediate, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 770229.78

構造登録者

Schnell, H.M.,Walsh Jr, R.M.,Rawson, S.,Hanna, J.W. (登録日: 2021-02-17, 公開日: 2021-04-14, 最終更新日: 2024-03-06)

主引用文献

Schnell, H.M.,Walsh Jr., R.M.,Rawson, S.,Kaur, M.,Bhanu, M.K.,Tian, G.,Prado, M.A.,Guerra-Moreno, A.,Paulo, J.A.,Gygi, S.P.,Roelofs, J.,Finley, D.,Hanna, J.
Structures of chaperone-associated assembly intermediates reveal coordinated mechanisms of proteasome biogenesis.
Nat.Struct.Mol.Biol., 28:418-425, 2021

PubMed Abstract: The proteasome mediates most selective protein degradation. Proteolysis occurs within the 20S core particle (CP), a barrel-shaped chamber with an αββα configuration. CP biogenesis proceeds through an ordered multistep pathway requiring five chaperones, Pba1-4 and Ump1. Using Saccharomyces cerevisiae, we report high-resolution structures of CP assembly intermediates by cryogenic-electron microscopy. The first structure corresponds to the 13S particle, which consists of a complete α-ring, partial β-ring (β2-4), Ump1 and Pba1/2. The second structure contains two additional subunits (β5-6) and represents a later pre-15S intermediate. These structures reveal the architecture and positions of Ump1 and β2/β5 propeptides, with important implications for their functions. Unexpectedly, Pba1's N terminus extends through an open CP pore, accessing the CP interior to contact Ump1 and the β5 propeptide. These results reveal how the coordinated activity of Ump1, Pba1 and the active site propeptides orchestrate key aspects of CP assembly.

PubMed: 33846632
DOI: 10.1038/s41594-021-00583-9

実験手法

ELECTRON MICROSCOPY (2.74 Å)