5L4G

The human 26S proteasome at 3.9 A

これはPDB形式変換不可エントリーです。

5L4G の概要

• エントリーDOI: 10.2210/pdb5l4g/pdb
• EMDBエントリー: 4002
• 分子名称: Proteasome subunit alpha type-6, Proteasome subunit beta type-3, Proteasome subunit beta type-4, ... (23 entities in total)
• 機能のキーワード: proteostasis, 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: 34
• 化学式量合計: 1049264.89

構造登録者

Schweitzer, A.,Aufderheide, A.,Rudack, T.,Beck, F. (登録日: 2016-05-25, 公開日: 2016-09-07, 最終更新日: 2024-05-08)

主引用文献

Schweitzer, A.,Aufderheide, A.,Rudack, T.,Beck, F.,Pfeifer, G.,Plitzko, J.M.,Sakata, E.,Schulten, K.,Forster, F.,Baumeister, W.
Structure of the human 26S proteasome at a resolution of 3.9 angstrom.
Proc.Natl.Acad.Sci.USA, 113:7816-7821, 2016

PubMed Abstract: Protein degradation in eukaryotic cells is performed by the Ubiquitin-Proteasome System (UPS). The 26S proteasome holocomplex consists of a core particle (CP) that proteolytically degrades polyubiquitylated proteins, and a regulatory particle (RP) containing the AAA-ATPase module. This module controls access to the proteolytic chamber inside the CP and is surrounded by non-ATPase subunits (Rpns) that recognize substrates and deubiquitylate them before unfolding and degradation. The architecture of the 26S holocomplex is highly conserved between yeast and humans. The structure of the human 26S holocomplex described here reveals previously unidentified features of the AAA-ATPase heterohexamer. One subunit, Rpt6, has ADP bound, whereas the other five have ATP in their binding pockets. Rpt6 is structurally distinct from the other five Rpt subunits, most notably in its pore loop region. For Rpns, the map reveals two main, previously undetected, features: the C terminus of Rpn3 protrudes into the mouth of the ATPase ring; and Rpn1 and Rpn2, the largest proteasome subunits, are linked by an extended connection. The structural features of the 26S proteasome observed in this study are likely to be important for coordinating the proteasomal subunits during substrate processing.

PubMed: 27342858
DOI: 10.1073/pnas.1608050113

実験手法

ELECTRON MICROSCOPY (3.9 Å)