3MH5

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

3MH5 の概要

• エントリーDOI: 10.2210/pdb3mh5/pdb
• 関連するPDBエントリー: 3MH4 3MH6 3MH7
• 分子名称: Protease do, DIISOPROPYL PHOSPHONATE (3 entities in total)
• 機能のキーワード: degp, htra, protease, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P0C0V0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96216.45

構造登録者

Krojer, T.,Sawa, J.,Huber, R.,Clausen, T. (登録日: 2010-04-07, 公開日: 2010-06-30, 最終更新日: 2024-11-13)

主引用文献

Krojer, T.,Sawa, J.,Huber, R.,Clausen, T.
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
Nat.Struct.Mol.Biol., 17:844-852, 2010

PubMed Abstract: HtrA proteases are tightly regulated proteolytic assemblies that are essential for maintaining protein homeostasis in extracytosolic compartments. Though HtrA proteases have been characterized in detail, their precise molecular mechanism for switching between different functional states is still unknown. To address this, we carried out biochemical and structural studies of DegP from Escherichia coli. We show that effector-peptide binding to the PDZ domain of DegP induces oligomer conversion from resting hexameric DegP6 into proteolytically active 12-mers and 24-mers (DegP12/24). Moreover, our data demonstrate that a specific protease loop (L3) functions as a conserved molecular switch of HtrA proteases. L3 senses the activation signal-that is, the repositioned PDZ domain of substrate-engaged DegP12/24 or the binding of allosteric effectors to regulatory HtrA proteases such as DegS-and transmits this information to the active site. Implications for protein quality control and regulation of oligomeric enzymes are discussed.

PubMed: 20581825
DOI: 10.1038/nsmb.1840

実験手法

X-RAY DIFFRACTION (3 Å)