6PP6

ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3

6PP6 の概要

• エントリーDOI: 10.2210/pdb6pp6/pdb
• EMDBエントリー: 20406 20408 20412 20418 20419 20420
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpX, substrate peptide, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 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; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 242721.00

構造登録者

Fei, X.,Jenni, S.,Harrison, S.C.,Sauer, R.T. (登録日: 2019-07-05, 公開日: 2020-03-11, 最終更新日: 2024-03-20)

主引用文献

Fei, X.,Bell, T.A.,Jenni, S.,Stinson, B.M.,Baker, T.A.,Harrison, S.C.,Sauer, R.T.
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.
Elife, 9:-, 2020

PubMed Abstract: ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the enzyme that show how asymmetric hexameric rings of ClpX bind symmetric heptameric rings of ClpP and interact with protein substrates. Subunits in the ClpX hexamer assume a spiral conformation and interact with two-residue segments of substrate in the axial channel, as observed for other AAA+ proteases and protein-remodeling machines. Strictly sequential models of ATP hydrolysis and a power stroke that moves two residues of the substrate per translocation step have been inferred from these structural features for other AAA+ unfoldases, but biochemical and single-molecule biophysical studies indicate that ClpXP operates by a probabilistic mechanism in which five to eight residues are translocated for each ATP hydrolyzed. We propose structure-based models that could account for the functional results.

PubMed: 32108573
DOI: 10.7554/eLife.52774

実験手法

ELECTRON MICROSCOPY (4.28 Å)