2QGR

Structure of the R178A mutant of delta PDZ DegS protease

2QGR の概要

• エントリーDOI: 10.2210/pdb2qgr/pdb
• 関連するPDBエントリー: 2QF0 2QF3
• 分子名称: Protease degS (1 entity in total)
• 機能のキーワード: degs, protease, periplasmic stress sensor, htra, allosteric activation, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26048.33

構造登録者

Sohn, J.,Grant, R.A.,Sauer, R.T. (登録日: 2007-06-29, 公開日: 2007-12-11, 最終更新日: 2023-08-30)

主引用文献

Sohn, J.,Grant, R.A.,Sauer, R.T.
Allosteric activation of DegS, a stress sensor PDZ protease.
Cell(Cambridge,Mass.), 131:572-583, 2007

PubMed Abstract: Regulated intramembrane proteolysis is a method for transducing signals between cellular compartments. When protein folding is compromised in the periplasm of E. coli, the C termini of outer-membrane proteins (OMPs) bind to the PDZ domains of the trimeric DegS protease and activate cleavage of RseA, a transmembrane transcriptional regulator. We show here that DegS is an allosteric enzyme. OMP binding shifts the equilibrium from a nonfunctional state, in which the active sites are unreactive, to the functional proteolytic conformation. Crystallographic, biochemical, and mutagenic experiments show that the unliganded PDZ domains are inhibitory and suggest that OMP binding per se is sufficient to stabilize the relaxed conformation and activate DegS. OMP-induced activation and RseA binding are both positively cooperative, allowing switch-like behavior of the OMP-DegS-RseA system. Residues involved in the DegS allosteric switch are conserved in the DegP/HtrA and HtrA2/Omi families, suggesting that many PDZ proteases use a common mechanism of allosteric activation.

PubMed: 17981123
DOI: 10.1016/j.cell.2007.08.044

実験手法

X-RAY DIFFRACTION (2.7 Å)