6WR2

ClpP and ClpX IGF loop in ClpX-ClpP complex bound to ssrA tagged GFP

6WR2 の概要

• エントリーDOI: 10.2210/pdb6wr2/pdb
• EMDBエントリー: 21875
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpX, ATP-dependent Clp protease proteolytic subunit (3 entities in total)
• 機能のキーワード: protein degradation, aaa+ protease complex, chaperone
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 582699.04

構造登録者

Fei, X.,Sauer, R.T. (登録日: 2020-04-29, 公開日: 2020-11-04, 最終更新日: 2024-03-06)

主引用文献

Fei, X.,Bell, T.A.,Barkow, S.R.,Baker, T.A.,Sauer, R.T.
Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates.
Elife, 9:-, 2020

PubMed Abstract: When ribosomes fail to complete normal translation, all cells have mechanisms to ensure degradation of the resulting partial proteins to safeguard proteome integrity. In and other eubacteria, the tmRNA system rescues stalled ribosomes and adds an ssrA tag or degron to the C-terminus of the incomplete protein, which directs degradation by the AAA+ ClpXP protease. Here, we present cryo-EM structures of ClpXP bound to the ssrA degron. C-terminal residues of the ssrA degron initially bind in the top of an otherwise closed ClpX axial channel and subsequently move deeper into an open channel. For short-degron protein substrates, we show that unfolding can occur directly from the initial closed-channel complex. For longer degron substrates, our studies illuminate how ClpXP transitions from specific recognition into a nonspecific unfolding and translocation machine. Many AAA+ proteases and protein-remodeling motors are likely to employ similar multistep recognition and engagement strategies.

PubMed: 33089779
DOI: 10.7554/eLife.61496

実験手法

ELECTRON MICROSCOPY (2.88 Å)