7UJ0

ClpAP complex bound to ClpS N-terminal extension, class IIIb

7UJ0 の概要

• エントリーDOI: 10.2210/pdb7uj0/pdb
• EMDBエントリー: 26554 26555 26556 26557 26558 26559
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpA, ATP-dependent Clp protease adapter protein ClpS, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total)
• 機能のキーワード: aaa+ protease, adaptor, protein complex, chaperone
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 682581.19

構造登録者

Kim, S.,Fei, X.,Sauer, R.T.,Baker, T.A. (登録日: 2022-03-29, 公開日: 2022-11-09, 最終更新日: 2024-06-12)

主引用文献

Kim, S.,Fei, X.,Sauer, R.T.,Baker, T.A.
AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
Nat.Struct.Mol.Biol., 29:1068-1079, 2022

PubMed Abstract: ClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor. Here we present high-resolution cryo-EM structures of Escherichia coli ClpAPS complexes, showing how ClpA pore loops interact with the ClpS N-terminal extension (NTE), which is normally intrinsically disordered. In two classes, the NTE is bound by a spiral of pore-1 and pore-2 loops in a manner similar to substrate-polypeptide binding by many AAA+ unfoldases. Kinetic studies reveal that pore-2 loops of the ClpA D1 ring catalyze the protein remodeling required for substrate delivery by ClpS. In a third class, D2 pore-1 loops are rotated, tucked away from the channel and do not bind the NTE, demonstrating asymmetry in engagement by the D1 and D2 rings. These studies show additional structures and functions for key AAA+ elements. Pore-loop tucking may be used broadly by AAA+ unfoldases, for example, during enzyme pausing/unloading.

PubMed: 36329286
DOI: 10.1038/s41594-022-00850-3

実験手法

ELECTRON MICROSCOPY (3.26 Å)