6EW9

CRYSTAL STRUCTURE OF DEGS STRESS SENSOR PROTEASE IN COMPLEX WITH ACTIVATING DNRLGLVYQF PEPTIDE

6EW9 の概要

• エントリーDOI: 10.2210/pdb6ew9/pdb
• 分子名称: Serine endoprotease DegS, DNRLGLVYQF PEPTIDE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: protease, stress-sensor, pdz, hydrolase, periplasm, serine proteiase, activator peptide
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 103902.76

構造登録者

Vetter, I.R.,Porfetye, A.T.,Stege, P. (登録日: 2017-11-03, 公開日: 2018-04-25, 最終更新日: 2024-05-08)

主引用文献

Bongard, J.,Lorenz, M.,Vetter, I.R.,Stege, P.,Porfetye, A.T.,Schmitz, A.L.,Kaschani, F.,Wolf, A.,Koch, U.,Nussbaumer, P.,Klebl, B.,Kaiser, M.,Ehrmann, M.
Identification of Noncatalytic Lysine Residues from Allosteric Circuits via Covalent Probes.
ACS Chem. Biol., 13:1307-1312, 2018

PubMed Abstract: Covalent modifications of nonactive site lysine residues by small molecule probes has recently evolved into an important strategy for interrogating biological systems. Here, we report the discovery of a class of bioreactive compounds that covalently modify lysine residues in DegS, the rate limiting protease of the essential bacterial outer membrane stress response pathway. These modifications lead to an allosteric activation and allow the identification of novel residues involved in the allosteric activation circuit. These findings were validated by structural analyses via X-ray crystallography and cell-based reporter systems. We anticipate that our findings are not only relevant for a deeper understanding of the structural basis of allosteric activation in DegS and other HtrA serine proteases but also pinpoint an alternative use of covalent small molecules for probing essential biochemical mechanisms.

PubMed: 29658704
DOI: 10.1021/acschembio.8b00101

実験手法

X-RAY DIFFRACTION (2.2 Å)