3MT6

Structure of ClpP from Escherichia coli in complex with ADEP1

3MT6 の概要

• エントリーDOI: 10.2210/pdb3mt6/pdb
• 関連するPDBエントリー: 1TYF 1Y7O 1YG6 2FZS 3KTG 3KTH 3KTI 3KTJ 3KTK
• 関連するBIRD辞書のPRD_ID: PRD_000503
• 分子名称: ATP-dependent Clp protease proteolytic subunit, ACYLDEPSIPEPTIDE 1, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: endopeptidase clp, caseinolytic protease, protease ti, acypdepsipeptide antibiotics, hydrolase-antibiotic complex, hydrolase/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P0A6G7
• タンパク質・核酸の鎖数: 56
• 化学式量合計: 677085.71

構造登録者

Chung, Y.S. (登録日: 2010-04-30, 公開日: 2010-11-03, 最終更新日: 2023-11-22)

主引用文献

Li, D.H.,Chung, Y.S.,Gloyd, M.,Joseph, E.,Ghirlando, R.,Wright, G.D.,Cheng, Y.Q.,Maurizi, M.R.,Guarne, A.,Ortega, J.
Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
Chem.Biol., 17:959-969, 2010

PubMed Abstract: In ClpXP and ClpAP complexes, ClpA and ClpX use the energy of ATP hydrolysis to unfold proteins and translocate them into the self-compartmentalized ClpP protease. ClpP requires the ATPases to degrade folded or unfolded substrates, but binding of acyldepsipeptide antibiotics (ADEPs) to ClpP bypasses this requirement with unfolded proteins. We present the crystal structure of Escherichia coli ClpP bound to ADEP1 and report the structural changes underlying ClpP activation. ADEP1 binds in the hydrophobic groove that serves as the primary docking site for ClpP ATPases. Binding of ADEP1 locks the N-terminal loops of ClpP in a β-hairpin conformation, generating a stable pore through which extended polypeptides can be threaded. This structure serves as a model for ClpP in the holoenzyme ClpAP and ClpXP complexes and provides critical information to further develop this class of antibiotics.

PubMed: 20851345
DOI: 10.1016/j.chembiol.2010.07.008

実験手法

X-RAY DIFFRACTION (1.901 Å)