3GCO

Crystal structure of DegS H198P/D320A mutant modified by DFP in complex with DNRDGNVYQF OMP peptide

3GCO の概要

• エントリーDOI: 10.2210/pdb3gco/pdb
• 関連するPDBエントリー: 3GCN 3GDS 3GDU 3GDV
• 分子名称: Protease degS, DNRDGNVYQF peptide (2 entities in total)
• 機能のキーワード: protease, stress-sensor, htra, pdz omp, allostery, hydrolase, serine protease, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Single-pass membrane protein : P0AEE3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37486.04

構造登録者

Sohn, J.,Grant, R.A.,Sauer, R.T. (登録日: 2009-02-22, 公開日: 2009-03-31, 最終更新日: 2021-10-20)

主引用文献

Sohn, J.,Grant, R.A.,Sauer, R.T.
OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism.
Structure, 17:1411-1421, 2009

PubMed Abstract: In the E. coli periplasm, C-terminal peptides of misfolded outer-membrane porins (OMPs) bind to the PDZ domains of the trimeric DegS protease, triggering cleavage of a transmembrane regulator and transcriptional activation of stress genes. We show that an active-site DegS mutation partially bypasses the requirement for peptide activation and acts synergistically with mutations that disrupt contacts between the protease and PDZ domains. Biochemical results support an allosteric model, in which these mutations, active-site modification, and peptide/substrate binding act in concert to stabilize proteolytically active DegS. Cocrystal structures of DegS in complex with different OMP peptides reveal activation of the protease domain with varied conformations of the PDZ domain and without specific contacts from the bound OMP peptide. Taken together, these results indicate that the binding of OMP peptides activates proteolysis principally by relieving inhibitory contacts between the PDZ domain and the protease domain of DegS.

PubMed: 19836340
DOI: 10.1016/j.str.2009.07.017

実験手法

X-RAY DIFFRACTION (2.798 Å)