1SOZ

Crystal Structure of DegS protease in complex with an activating peptide

Summary for 1SOZ

• Entry DOI: 10.2210/pdb1soz/pdb
• Related: 1SOT 1VCW
• Descriptor: Protease degS, activating peptide (3 entities in total)
• Functional Keywords: stress response, protein quality control, pdz, upr, htra, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm (Potential): P31137
• Total number of polymer chains: 5
• Total formula weight: 102181.74

Authors

Wilken, C.,Kitzing, K.,Kurzbauer, R.,Ehrmann, M.,Clausen, T. (deposition date: 2004-03-16, release date: 2004-06-08, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)