1soz: Difference between revisions

Revision as of 19:17, 27 July 2008

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File:1soz.png

Template:STRUCTURE 1soz

Crystal Structure of DegS protease in complex with an activating peptideCrystal Structure of DegS protease in complex with an activating peptide

Template:ABSTRACT PUBMED 15137941

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

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OCA

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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===
-==Overview==
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-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.
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 [[Category: Stress response]]
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