4rr0: Difference between revisions
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==re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE== | ==re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE== | ||
<StructureSection load='4rr0' size='340' side='right' caption='[[4rr0]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='4rr0' size='340' side='right'caption='[[4rr0]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rr0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RR0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rr0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RR0 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vcw|1vcw]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vcw|1vcw]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">degS, P12B_c3347 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4rr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr0 OCA], [http://pdbe.org/4rr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rr0 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr0 ProSAT]</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=4rr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr0 OCA], [http://pdbe.org/4rr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rr0 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | |||
[[Category: Grant, R A]] | [[Category: Grant, R A]] | ||
[[Category: Sauer, R T]] | [[Category: Sauer, R T]] | ||
Revision as of 13:36, 1 May 2019
re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDEre-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE
Structural highlights
Publication Abstract from PubMedGram-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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