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6LSY

AAA+ ATPase, ClpL from Streptococcus pneumoniae - ATP bound

これはPDB形式変換不可エントリーです。
6LSY の概要
エントリーDOI10.2210/pdb6lsy/pdb
EMDBエントリー0965
分子名称ATP-dependent Clp protease, ATP-binding subunit (1 entity in total)
機能のキーワードaaa+ atpase, chaperone, streptococcus pneumoniae
由来する生物種Streptococcus pneumoniae
タンパク質・核酸の鎖数14
化学式量合計1086387.32
構造登録者
Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S. (登録日: 2020-01-20, 公開日: 2021-01-27, 最終更新日: 2024-03-27)
主引用文献Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S.
ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric/dodecameric ones.
Faseb J., 34:14353-14370, 2020
Cited by
PubMed Abstract: AAA+ (ATPases associated with diverse cellular activities) chaperones are involved in a plethora of cellular activities to ensure protein homeostasis. The function of AAA+ chaperones is mostly modulated by their hexameric/dodecameric quaternary structures. Here we report the structural and biochemical characterizations of a tetradecameric AAA+ chaperone, ClpL from Streptococcus pneumoniae. ClpL exists as a tetradecamer in solution in the presence of ATP. The cryo-EM structure of ClpL at 4.5 Å resolution reveals a striking tetradecameric arrangement. Solution structures of ClpL derived from small-angle X-ray scattering data suggest that the tetradecameric ClpL could assume a spiral conformation found in active hexameric/dodecameric AAA+ chaperone structures. Vertical positioning of the middle domain accounts for the head-to-head arrangement of two heptameric rings. Biochemical activity assays with site-directed mutagenesis confirmed the critical roles of residues both in the integrity of the tetradecameric arrangement and activities of ClpL. Non-conserved Q321 and R670 are crucial in the heptameric ring assembly of ClpL. These results establish that ClpL is a functionally active tetradecamer, clearly distinct from hexameric/dodecameric AAA+ chaperones.
PubMed: 32910525
DOI: 10.1096/fj.202000843R
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (6.33 Å)
構造検証レポート
Validation report summary of 6lsy
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2026-04-29に公開中

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