1soz: Difference between revisions

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[[Image:1soz.gif|left|200px]]<br /><applet load="1soz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1soz.gif|left|200px]]<br /><applet load="1soz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1soz, resolution 2.4Å" />

'''Crystal Structure of DegS protease in complex with an activating peptide'''<br />

==Overview==

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.

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 Structure==

1SOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SOZ OCA].

1SOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOZ OCA].

==Reference==

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[[Category: upr]]

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@@ Line 1: / Line 1: @@
-[[Image:1soz.gif|left|200px]]<br /><applet load="1soz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1soz.gif|left|200px]]<br /><applet load="1soz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1soz, resolution 2.4&Aring;" />
 '''Crystal Structure of DegS protease in complex with an activating peptide'''<br />
 ==Overview==
-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.
+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 Structure==
-SOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SOZ OCA].
+SOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOZ OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: upr]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:32:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:44 2008''