2qf0

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[[Image:2qf0.jpg|left|200px]]
[[Image:2qf0.jpg|left|200px]]
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{{Structure
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|PDB= 2qf0 |SIZE=350|CAPTION= <scene name='initialview01'>2qf0</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2qf0", creates the "Structure Box" on the page.
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|GENE= degS, hhoB, htrH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_2qf0| PDB=2qf0 | SCENE= }}
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|RELATEDENTRY=[[2qf3|2QF3]], [[2qgr|2QGR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qf0 OCA], [http://www.ebi.ac.uk/pdbsum/2qf0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qf0 RCSB]</span>
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'''Structure of the delta PDZ truncation of the DegS protease'''
'''Structure of the delta PDZ truncation of the DegS protease'''
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[[Category: Sauer, R T.]]
[[Category: Sauer, R T.]]
[[Category: Sohn, J.]]
[[Category: Sohn, J.]]
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[[Category: allosteric activation]]
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[[Category: Allosteric activation]]
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[[Category: deg]]
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[[Category: Deg]]
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[[Category: htra]]
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[[Category: Htra]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: periplasmic stress sensor]]
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[[Category: Periplasmic stress sensor]]
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[[Category: protease]]
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[[Category: Protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:50:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:48:33 2008''
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Revision as of 11:50, 4 May 2008

Template:STRUCTURE 2qf0

Structure of the delta PDZ truncation of the DegS protease


Overview

Regulated intramembrane proteolysis is a method for transducing signals between cellular compartments. When protein folding is compromised in the periplasm of E. coli, the C termini of outer-membrane proteins (OMPs) bind to the PDZ domains of the trimeric DegS protease and activate cleavage of RseA, a transmembrane transcriptional regulator. We show here that DegS is an allosteric enzyme. OMP binding shifts the equilibrium from a nonfunctional state, in which the active sites are unreactive, to the functional proteolytic conformation. Crystallographic, biochemical, and mutagenic experiments show that the unliganded PDZ domains are inhibitory and suggest that OMP binding per se is sufficient to stabilize the relaxed conformation and activate DegS. OMP-induced activation and RseA binding are both positively cooperative, allowing switch-like behavior of the OMP-DegS-RseA system. Residues involved in the DegS allosteric switch are conserved in the DegP/HtrA and HtrA2/Omi families, suggesting that many PDZ proteases use a common mechanism of allosteric activation.

About this Structure

2QF0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Allosteric activation of DegS, a stress sensor PDZ protease., Sohn J, Grant RA, Sauer RT, Cell. 2007 Nov 2;131(3):572-83. PMID:17981123 Page seeded by OCA on Sun May 4 14:50:38 2008

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