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'''Crystal Structure of DegS protease in complex with an activating peptide''' | '''Crystal Structure of DegS protease in complex with an activating peptide''' | ||
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[[Category: Kurzbauer, R.]] | [[Category: Kurzbauer, R.]] | ||
[[Category: Wilken, C.]] | [[Category: Wilken, C.]] | ||
[[Category: | [[Category: Htra]] | ||
[[Category: | [[Category: Pdz]] | ||
[[Category: | [[Category: Protein quality control]] | ||
[[Category: | [[Category: Stress response]] | ||
[[Category: | [[Category: Upr]] | ||
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Revision as of 08:58, 3 May 2008
Crystal Structure of DegS protease in complex with an activating peptide
OverviewOverview
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.
About this StructureAbout this Structure
1SOZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease., Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T, Cell. 2004 May 14;117(4):483-94. PMID:15137941 Page seeded by OCA on Sat May 3 08:58:10 2008