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6EM9

S.aureus ClpC resting state, asymmetric map

6EM9 の概要
エントリーDOI10.2210/pdb6em9/pdb
EMDBエントリー3894 3895
分子名称ATP-dependent Clp protease ATP-binding subunit ClpC (1 entity in total)
機能のキーワードclpc, aaa+ protease, oligomeric complex, chaperone
由来する生物種Staphylococcus aureus (strain bovine RF122 / ET3-1)
タンパク質・核酸の鎖数10
化学式量合計912003.75
構造登録者
Carroni, M.,Mogk, A.,Bukau, B.,Franke, K. (登録日: 2017-10-01, 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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (8.4 Å)
構造検証レポート
Validation report summary of 6em9
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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