3KTH

Structure of ClpP from Bacillus subtilis in orthorombic crystal form

3KTH の概要

• エントリーDOI: 10.2210/pdb3kth/pdb
• 関連するPDBエントリー: 3KTG 3KTI 3KTJ 3KTK
• 分子名称: ATP-dependent Clp protease proteolytic subunit (2 entities in total)
• 機能のキーワード: hydrolase, atp-binding, nucleotide-binding, protease, serine protease, stress response
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (By similarity): P80244
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 154302.89

構造登録者

Lee, B.-G.,Brotz-Oesterhelt, H.,Song, H.K. (登録日: 2009-11-25, 公開日: 2010-03-23, 最終更新日: 2024-05-29)

主引用文献

Lee, B.-G.,Park, E.Y.,Lee, K.-E.,Jeon, H.,Sung, K.H.,Paulsen, H.,Rubsamen-Schaeff, H.,Brotz-Oesterhelt, H.,Song, H.K.
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Nat.Struct.Mol.Biol., 17:471-478, 2010

PubMed Abstract: Clp-family proteins are prototypes for studying the mechanism of ATP-dependent proteases because the proteolytic activity of the ClpP core is tightly regulated by activating Clp-ATPases. Nonetheless, the proteolytic activation mechanism has remained elusive because of the lack of a complex structure. Acyldepsipeptides (ADEPs), a recently discovered class of antibiotics, activate and disregulate ClpP. Here we have elucidated the structural changes underlying the ClpP activation process by ADEPs. We present the structures of Bacillus subtilis ClpP alone and in complex with ADEP1 and ADEP2. The structures show the closed-to-open-gate transition of the ClpP N-terminal segments upon activation as well as conformational changes restricted to the upper portion of ClpP. The direction of the conformational movement and the hydrophobic clustering that stabilizes the closed structure are markedly different from those of other ATP-dependent proteases, providing unprecedented insights into the activation of ClpP.

PubMed: 20305655
DOI: 10.1038/nsmb.1787

実験手法

X-RAY DIFFRACTION (3 Å)