4rr0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:54, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==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]] 3.05&Aring;' scene=''>
+
<StructureSection load='4rr0' size='340' side='right'caption='[[4rr0]], [[Resolution|resolution]] 3.05&Aring;' 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 [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.054&#8491;</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://www.rcsb.org/pdb/explore.do?structureId=4rr0 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr0 PDBsum]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr0 OCA], [https://pdbe.org/4rr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rr0 RCSB], [https://www.ebi.ac.uk/pdbsum/4rr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr0 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://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>
-
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.
+
-
 
+
-
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<ref>PMID:15137941</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Grant, R A]]
+
[[Category: Escherichia coli]]
-
[[Category: Sauer, R T]]
+
[[Category: Large Structures]]
-
[[Category: Htra]]
+
[[Category: Grant RA]]
-
[[Category: Hydrolase]]
+
[[Category: Sauer RT]]
-
[[Category: Pdz]]
+
-
[[Category: Protein quality control]]
+
-
[[Category: Stress response]]
+
-
[[Category: Upr]]
+

Current revision

re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE

PDB ID 4rr0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rr0"
Personal tools