6FVT

26S proteasome, s1 state

これはPDB形式変換不可エントリーです。

6FVT の概要

• エントリーDOI: 10.2210/pdb6fvt/pdb
• EMDBエントリー: 3534
• 分子名称: Proteasome subunit alpha type-1, Proteasome subunit beta type-3, Proteasome subunit beta type-4, ... (36 entities in total)
• 機能のキーワード: 26s proteasome, aaa+ atpase, 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: 47
• 化学式量合計: 1582559.36

構造登録者

Eisele, M.R.,Reed, R.G.,Rudack, T.,Schweitzer, A.,Beck, F.,Nagy, I.,Pfeifer, G.,Plitzko, J.M.,Baumeister, W.,Tomko, R.J.,Sakata, E. (登録日: 2018-03-05, 公開日: 2018-08-22, 最終更新日: 2024-05-08)

主引用文献

Eisele, M.R.,Reed, R.G.,Rudack, T.,Schweitzer, A.,Beck, F.,Nagy, I.,Pfeifer, G.,Plitzko, J.M.,Baumeister, W.,Tomko Jr., R.J.,Sakata, E.
Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.
Cell Rep, 24:1301-1315.e5, 2018

PubMed Abstract: The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrates into the proteolytic 20S core particle for degradation. Here, we combine genetic and biochemical approaches with cryo-electron microscopy and integrative modeling to dissect the relationship between individual nucleotide binding events and proteasome conformational dynamics. We demonstrate unique impacts of ATP binding by individual ATPases on the proteasome conformational distribution and report two conformational states of the proteasome suggestive of a rotary ATP hydrolysis mechanism. These structures, coupled with functional analyses, reveal key roles for the ATPases Rpt1 and Rpt6 in gating substrate entry into the core particle. This deepened knowledge of proteasome conformational dynamics reveals key elements of intersubunit communication within the proteasome and clarifies the regulation of substrate entry into the proteolytic chamber.

PubMed: 30067984
DOI: 10.1016/j.celrep.2018.07.004

実験手法

ELECTRON MICROSCOPY (4.1 Å)