6SFW

Cryo-EM Structure of the ClpX component of the ClpXP1/2 degradation machinery.

6SFW の概要

• エントリーDOI: 10.2210/pdb6sfw/pdb
• 関連するPDBエントリー: 6SFW 6SFX
• EMDBエントリー: 10162
• 分子名称: ATP-dependent Clp protease ATP-binding subunit ClpX (1 entity in total)
• 機能のキーワード: aaa+, atpase, protease, listeria, motor protein, chaperone, transport protein
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 278953.03

構造登録者

Gatsogiannis, C.,Merino, F.,Raunser, S. (登録日: 2019-08-02, 公開日: 2019-10-16, 最終更新日: 2024-05-15)

主引用文献

Gatsogiannis, C.,Balogh, D.,Merino, F.,Sieber, S.A.,Raunser, S.
Cryo-EM structure of the ClpXP protein degradation machinery.
Nat.Struct.Mol.Biol., 26:946-954, 2019

PubMed Abstract: The ClpXP machinery is a two-component protease complex that performs targeted protein degradation in bacteria and mitochondria. The complex consists of the AAA+ chaperone ClpX and the peptidase ClpP. The hexameric ClpX utilizes the energy of ATP binding and hydrolysis to engage, unfold and translocate substrates into the catalytic chamber of tetradecameric ClpP, where they are degraded. Formation of the complex involves a symmetry mismatch, because hexameric AAA+ rings bind axially to the opposing stacked heptameric rings of the tetradecameric ClpP. Here we present the cryo-EM structure of ClpXP from Listeria monocytogenes. We unravel the heptamer-hexamer binding interface and provide novel insight into the ClpX-ClpP cross-talk and activation mechanism. Comparison with available crystal structures of ClpP and ClpX in different states allows us to understand important aspects of the complex mode of action of ClpXP and provides a structural framework for future pharmacological applications.

PubMed: 31582852
DOI: 10.1038/s41594-019-0304-0

実験手法

ELECTRON MICROSCOPY (6 Å)