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3gdv

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Revision as of 07:03, 1 November 2017

Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide

Structural highlights

3gdv is a 6 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	3gds, 3gdu
Gene:	b3235, degS, hhoB, htrH, JW3204 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DEGS_ECOLI] When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMPs) and then initiates RseA (anti sigma-E factor) degradation by cleaving it in its periplasmic domain, making it an attractive substrate for subsequent cleavage by RseP. This cascade that ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In the E. coli periplasm, C-terminal peptides of misfolded outer-membrane porins (OMPs) bind to the PDZ domains of the trimeric DegS protease, triggering cleavage of a transmembrane regulator and transcriptional activation of stress genes. We show that an active-site DegS mutation partially bypasses the requirement for peptide activation and acts synergistically with mutations that disrupt contacts between the protease and PDZ domains. Biochemical results support an allosteric model, in which these mutations, active-site modification, and peptide/substrate binding act in concert to stabilize proteolytically active DegS. Cocrystal structures of DegS in complex with different OMP peptides reveal activation of the protease domain with varied conformations of the PDZ domain and without specific contacts from the bound OMP peptide. Taken together, these results indicate that the binding of OMP peptides activates proteolysis principally by relieving inhibitory contacts between the PDZ domain and the protease domain of DegS.

OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism.,Sohn J, Grant RA, Sauer RT Structure. 2009 Oct 14;17(10):1411-21. PMID:19836340^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Alba BM, Leeds JA, Onufryk C, Lu CZ, Gross CA. DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response. Genes Dev. 2002 Aug 15;16(16):2156-68. PMID:12183369 doi:10.1101/gad.1008902
↑ Meltzer M, Hasenbein S, Mamant N, Merdanovic M, Poepsel S, Hauske P, Kaiser M, Huber R, Krojer T, Clausen T, Ehrmann M. Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli. Res Microbiol. 2009 Nov;160(9):660-6. doi: 10.1016/j.resmic.2009.07.012. Epub, 2009 Aug 18. PMID:19695325 doi:10.1016/j.resmic.2009.07.012
↑ Sohn J, Grant RA, Sauer RT. OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure. 2009 Oct 14;17(10):1411-21. PMID:19836340 doi:10.1016/j.str.2009.07.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gdv"

@@ Line 1: / Line 1: @@
 ==Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide==
 <StructureSection load='3gdv' size='340' side='right' caption='[[3gdv]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gds|3gds]], [[3gdu|3gdu]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3235, degS, hhoB, htrH, JW3204 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdv OCA], [http://pdbe.org/3gdv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gdv RCSB], [http://www.ebi.ac.uk/pdbsum/3gdv PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdv OCA], [http://pdbe.org/3gdv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gdv RCSB], [http://www.ebi.ac.uk/pdbsum/3gdv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gdv ProSAT]</span></td></tr>
 </table>
 == Function ==

3gdv

From Proteopedia

Revision as of 07:03, 1 November 2017

Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YQF peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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