1VCW

Crystal structure of DegS after backsoaking the activating peptide

1VCW の概要

• エントリーDOI: 10.2210/pdb1vcw/pdb
• 関連するPDBエントリー: 1SOT 1SOZ
• 分子名称: Protease degS (1 entity in total)
• 機能のキーワード: stress response, protein quality control, pdz, upr, htra, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm (Potential): P31137
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 99730.99

構造登録者

Wilken, C.,Kitzing, K.,Kurzbauer, R.,Ehrmann, M.,Clausen, T. (登録日: 2004-03-16, 公開日: 2004-06-08, 最終更新日: 2023-12-27)

主引用文献

Wilken, C.,Kitzing, K.,Kurzbauer, R.,Ehrmann, M.,Clausen, T.
Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease.
Cell(Cambridge,Mass.), 117:483-494, 2004

PubMed Abstract: Gram-negative bacteria respond to misfolded proteins in the cell envelope with the sigmaE-driven expression of periplasmic proteases/chaperones. Activation of sigmaE is controlled by a proteolytic cascade that is initiated by the DegS protease. DegS senses misfolded protein in the periplasm, undergoes autoactivation, and cleaves the antisigma factor RseA. Here, we present the crystal structures of three distinct states of DegS from E. coli. DegS alone exists in a catalytically inactive form. Binding of stress-signaling peptides to its PDZ domain induces a series of conformational changes that activates protease function. Backsoaking of crystals containing the DegS-activator complex revealed the presence of an active/inactive hybrid structure and demonstrated the reversibility of activation. Taken together, the structural data illustrate in molecular detail how DegS acts as a periplasmic stress sensor. Our results suggest a novel regulatory role for PDZ domains and unveil a novel mechanism of reversible protease activation.

PubMed: 15137941
DOI: 10.1016/S0092-8674(04)00454-4

実験手法

X-RAY DIFFRACTION (3.05 Å)