1te0

From Proteopedia

(Difference between revisions)

Revision as of 13:13, 25 December 2014

Structural analysis of DegS, a stress sensor of the bacterial periplasm

Structural highlights

1te0 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DEGS, HHOB, HTRH, B3235, Z4594, ECS4108 (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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

Regulated proteolysis is a key event in transmembrane signalling between intracellular compartments. In Escherichia coli the membrane-bound protease DegS has been identified as the periplasmic stress sensor for unfolded outer membrane proteins (OMPs). DegS inititates a proteolytic cascade resulting in the release of sigmaE the transcription factor of periplasmic genes. The crystal structure of DegS protease reported at 2.2 A resolution reveals a trimeric complex with the monomeric protease domain in an inhibited state followed by the inhibitory PDZ domain. Noteably, domain architecture and communication of DegS are remarkably to homologous proteins known to date. Here the domain interface is mechanically locked by three intradomain salt bridges. Co-crystallisation trials in the presence of a 10-residue activating peptide did not result in significant structural intradomain shifts nor distortions in the crystal packing. These observations imply a mode of activation indicative of peptide-induced structural shifts imposed to the protease domain rather than disturbing the PDZ-protease interface.

Structural analysis of DegS, a stress sensor of the bacterial periplasm.,Zeth K FEBS Lett. 2004 Jul 2;569(1-3):351-8. PMID:15225661^[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
↑ Zeth K. Structural analysis of DegS, a stress sensor of the bacterial periplasm. FEBS Lett. 2004 Jul 2;569(1-3):351-8. PMID:15225661 doi:10.1016/j.febslet.2004.06.012

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/1te0"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1te0]] is a 2 chain structure with 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=1TE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TE0 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEGS, HHOB, HTRH, B3235, Z4594, ECS4108 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEGS, HHOB, HTRH, B3235, Z4594, ECS4108 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1te0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1te0 RCSB], [http://www.ebi.ac.uk/pdbsum/1te0 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=1te0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1te0 RCSB], [http://www.ebi.ac.uk/pdbsum/1te0 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DEGS_ECOLI 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.<ref>PMID:12183369</ref> <ref>PMID:19695325</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 31: @@
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Ravelli, R B.G.]]
+[[Category: Ravelli, R B.G]]
-[[Category: Zeth, K.]]
+[[Category: Zeth, K]]
 [[Category: Alpha-beta protein]]
 [[Category: Hydrolase]]

1te0

From Proteopedia

Revision as of 13:13, 25 December 2014

Structural analysis of DegS, a stress sensor of the bacterial periplasm

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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