6VFX

ClpXP from Neisseria meningitidis - Conformation B

6VFX の概要

• エントリーDOI: 10.2210/pdb6vfx/pdb
• 関連するPDBエントリー: 6VFS
• EMDBエントリー: 21187 21194
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpX, Unidentified peptide substrate, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total)
• 機能のキーワード: complex, aaa+, protease, clpp, clpx, hydrolase
• 由来する生物種: Neisseria meningitidis; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 592754.55

構造登録者

Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E. (登録日: 2020-01-06, 公開日: 2020-01-22, 最終更新日: 2024-03-06)

主引用文献

Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E.
A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
Elife, 9:-, 2020

PubMed Abstract: The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ClpXP is an important target for drug development against infectious diseases. Although structures are available for isolated ClpX and ClpP rings, it remains unknown how symmetry mismatched ClpX and ClpP work in tandem for processive substrate translocation into the ClpP proteolytic chamber. Here, we present cryo-EM structures of the substrate-bound ClpXP complex from at 2.3 to 3.3 Å resolution. The structures allow development of a model in which the sequential hydrolysis of ATP is coupled to motions of ClpX loops that lead to directional substrate translocation and ClpX rotation relative to ClpP. Our data add to the growing body of evidence that AAA+ molecular machines generate translocating forces by a common mechanism.

PubMed: 31916936
DOI: 10.7554/eLife.52158

実験手法

ELECTRON MICROSCOPY (2.9 Å)