6EMW

Structure of S.aureus ClpC in complex with MecA

6EMW の概要

• エントリーDOI: 10.2210/pdb6emw/pdb
• EMDBエントリー: 3895 3897
• 分子名称: ATP-dependent Clp protease ATP-binding subunit, Class III stress response-related ATPase, AAA+ superfamily, ATP-dependent Clp protease ATP-binding subunit ClpC, ... (7 entities in total)
• 機能のキーワード: chaperone, aaa+ protein, unfoldase
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 42
• 化学式量合計: 632280.22

構造登録者

Carroni, M.,Mogk, A.,Bukau, B.,Franke, K. (登録日: 2017-10-03, 公開日: 2017-12-27, 最終更新日: 2024-05-15)

主引用文献

Carroni, M.,Franke, K.B.,Maurer, M.,Jager, J.,Hantke, I.,Gloge, F.,Linder, D.,Gremer, S.,Turgay, K.,Bukau, B.,Mogk, A.
Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.
Elife, 6:-, 2017

PubMed Abstract: Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. The adaptor MecA activates ClpC by targeting substrates and stimulating ClpC ATPase activity. We show how ClpC is repressed in its ground state by determining ClpC cryo-EM structures with and without MecA. ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs). MecA converts this resting state to an active planar ring structure by binding to MD interaction sites. Loss of ClpC repression in MD mutants causes constitutive activation and severe cellular toxicity. These findings unravel an unexpected regulatory concept executed by coiled-coil MDs to tightly control AAA+ chaperone activity.

PubMed: 29165246
DOI: 10.7554/eLife.30120

実験手法

ELECTRON MICROSCOPY (11 Å)