3lgi - Revision history

OCA at 10:20, 21 February 2024

OCA — Wed, 21 Feb 2024 10:20:28 GMT

←Older revision		Revision as of 10:20, 21 February 2024
Line 1:		Line 1:

	==Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A==		==Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A==
-	<StructureSection load='3lgi' size='340' side='right' caption='[[3lgi]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='3lgi' size='340' side='right'caption='[[3lgi]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lgi]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LGI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lgi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LGI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 1.652Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2qf3\|2qf3]]~~, [[~~3lgt~~\|~~3lgt]], [[3lgu\|3lgu]], [[3lgv\|3lgv]], [[3lgw\|3lgw]], [[3lgy\|3lgy]], [[3lh1\|3lh1]], [[3lh3\|3lh3~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [https://pdbe.org/3lgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [https://www.ebi.ac.uk/pdbsum/3lgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgi 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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [~~http~~://pdbe.org/3lgi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3lgi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgi ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== 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>	+	[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lgi ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lgi ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DegS is a periplasmic Escherichia coli protease, which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm. Each DegS subunit consists of a protease domain and a PDZ domain. During protein folding stress, DegS is allosterically activated by peptides exposed in misfolded outer membrane porins, which bind to the PDZ domain and stabilize the active protease. It is not known whether allostery is conferred by the PDZ domains or is an intrinsic feature of the trimeric protease domain. Here, we demonstrate that free DegS(DeltaPDZ) equilibrates between active and inactive trimers with the latter species predominating. Substrate binding stabilizes active DegS(DeltaPDZ) in a positively cooperative fashion. Mutations can also stabilize active DegS(DeltaPDZ) and produce an enzyme that displays hyperbolic kinetics and degrades substrate with a maximal velocity within error of that for fully activated, intact DegS. Crystal structures of multiple DegS(DeltaPDZ) variants, in functional and non-functional conformations, support a two-state model in which allosteric switching is mediated by changes in specific elements of tertiary structure in the context of an invariant trimeric base. Overall, our results indicate that protein substrates must bind sufficiently tightly and specifically to the functional conformation of DegS(DeltaPDZ) to assist their own degradation. Thus, substrate binding alone may have regulated the activities of ancestral DegS trimers with subsequent fusion of the protease domain to a PDZ domain, resulting in ligand-mediated regulation.
-
-	Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.,Sohn J, Grant RA, Sauer RT J Biol Chem. 2010 Oct 29;285(44):34039-47. Epub 2010 Aug 24. PMID:20739286<ref>PMID:20739286</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3lgi" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Grant, R A~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Sauer, R T~~]]	+	[[Category: Grant RA]]
-	[[Category: ~~Sohn, J~~]]	+	[[Category: Sauer RT]]
-	[[Category: ~~Htra]]~~	+	[[Category: Sohn J]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Pdz omp]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Serine protease]]~~	+
-	~~[[Category: Stress-sensor~~]]	+

OCA at 19:25, 24 January 2018

OCA — Wed, 24 Jan 2018 19:25:09 GMT

←Older revision		Revision as of 19:25, 24 January 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lgi_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lgi_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 06:16, 5 August 2016

OCA — Fri, 05 Aug 2016 06:16:41 GMT

←Older revision		Revision as of 06:16, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A==		==Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A==
	<StructureSection load='3lgi' size='340' side='right' caption='[[3lgi]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='3lgi' size='340' side='right' caption='[[3lgi]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lgi]] is a 3 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=3LGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lgi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2qf3\|2qf3]], [[3lgt\|3lgt]], [[3lgu\|3lgu]], [[3lgv\|3lgv]], [[3lgw\|3lgw]], [[3lgy\|3lgy]], [[3lh1\|3lh1]], [[3lh3\|3lh3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2qf3\|2qf3]], [[3lgt\|3lgt]], [[3lgu\|3lgu]], [[3lgv\|3lgv]], [[3lgw\|3lgw]], [[3lgy\|3lgy]], [[3lh1\|3lh1]], [[3lh3\|3lh3]]</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=~~562 Escherichia coli~~])</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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [http://www.ebi.ac.uk/pdbsum/3lgi 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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [http://pdbe.org/3lgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [http://www.ebi.ac.uk/pdbsum/3lgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lgi ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3lgi" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Grant, R A]]		[[Category: Grant, R A]]
	[[Category: Sauer, R T]]		[[Category: Sauer, R T]]

OCA at 16:27, 25 December 2014

OCA — Thu, 25 Dec 2014 16:27:07 GMT

←Older revision		Revision as of 16:27, 25 December 2014
Line 8:		Line 8:
	<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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [http://www.ebi.ac.uk/pdbsum/3lgi 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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [http://www.ebi.ac.uk/pdbsum/3lgi 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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 17:12, 18 December 2014

OCA — Thu, 18 Dec 2014 17:12:36 GMT

←Older revision		Revision as of 17:12, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3lgi\| PDB=3lgi \| SCENE= }}~~	+	==Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A==
-	===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===	+	<StructureSection load='3lgi' size='340' side='right' caption='[[3lgi]], [[Resolution\|resolution]] 1.65Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20739286}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lgi]] is a 3 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=3LGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGI FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2qf3\|2qf3]], [[3lgt\|3lgt]], [[3lgu\|3lgu]], [[3lgv\|3lgv]], [[3lgw\|3lgw]], [[3lgy\|3lgy]], [[3lh1\|3lh1]], [[3lh3\|3lh3]]</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=562 Escherichia coli])</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=3lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lgi RCSB], [http://www.ebi.ac.uk/pdbsum/3lgi PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lgi_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DegS is a periplasmic Escherichia coli protease, which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm. Each DegS subunit consists of a protease domain and a PDZ domain. During protein folding stress, DegS is allosterically activated by peptides exposed in misfolded outer membrane porins, which bind to the PDZ domain and stabilize the active protease. It is not known whether allostery is conferred by the PDZ domains or is an intrinsic feature of the trimeric protease domain. Here, we demonstrate that free DegS(DeltaPDZ) equilibrates between active and inactive trimers with the latter species predominating. Substrate binding stabilizes active DegS(DeltaPDZ) in a positively cooperative fashion. Mutations can also stabilize active DegS(DeltaPDZ) and produce an enzyme that displays hyperbolic kinetics and degrades substrate with a maximal velocity within error of that for fully activated, intact DegS. Crystal structures of multiple DegS(DeltaPDZ) variants, in functional and non-functional conformations, support a two-state model in which allosteric switching is mediated by changes in specific elements of tertiary structure in the context of an invariant trimeric base. Overall, our results indicate that protein substrates must bind sufficiently tightly and specifically to the functional conformation of DegS(DeltaPDZ) to assist their own degradation. Thus, substrate binding alone may have regulated the activities of ancestral DegS trimers with subsequent fusion of the protease domain to a PDZ domain, resulting in ligand-mediated regulation.

-	~~==Function==~~	+	Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.,Sohn J, Grant RA, Sauer RT J Biol Chem. 2010 Oct 29;285(44):34039-47. Epub 2010 Aug 24. PMID:20739286<ref>PMID:20739286</ref>
-	~~[[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3lgi]] is~~ a ~~3 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=3LGI OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020739286</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Grant, R A..]]	+	[[Category: Grant, R A]]
-	[[Category: Sauer, R T.]]	+	[[Category: Sauer, R T]]
-	[[Category: Sohn, J.]]	+	[[Category: Sohn, J]]
	[[Category: Htra]]		[[Category: Htra]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA: Protected "3lgi" [edit=sysop:move=sysop]

OCA — Thu, 04 Apr 2013 20:27:01 GMT

Protected "3lgi" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:27, 4 April 2013

OCA at 20:26, 4 April 2013

OCA — Thu, 04 Apr 2013 20:26:59 GMT

←Older revision		Revision as of 20:26, 4 April 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:3lgi.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3lgi", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3lgi\| PDB=3lgi \| SCENE= }}		{{STRUCTURE_3lgi\| PDB=3lgi \| SCENE= }}
-
	===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===		===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===
		+	{{ABSTRACT_PUBMED_20739286}}

-		+	==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>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20739286}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 20739286 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20739286}}~~	+

	==About this Structure==		==About this Structure==
-	~~3LGI~~ is a 3 ~~chains~~ structure with ~~sequences~~ 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=3LGI OCA].	+	[[3lgi]] is a 3 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=3LGI OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20739286~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020739286</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Grant, R A..]]		[[Category: Grant, R A..]]
Line 34:		Line 21:
	[[Category: Serine protease]]		[[Category: Serine protease]]
	[[Category: Stress-sensor]]		[[Category: Stress-sensor]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:55:17 2010''

OCA at 03:44, 10 November 2010

OCA — Wed, 10 Nov 2010 03:44:23 GMT

←Older revision		Revision as of 03:44, 10 November 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3lgi.~~jpg~~\|left\|200px]]	+	[[Image:3lgi.png\|left\|200px]]

	<!--		<!--
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	===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===		===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20739286}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20739286 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20739286}}

	==About this Structure==		==About this Structure==
	3LGI is a 3 chains structure with sequences 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=3LGI OCA].		3LGI is a 3 chains structure with sequences 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=3LGI OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20739286</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Grant, R A..]]		[[Category: Grant, R A..]]
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	[[Category: Stress-sensor]]		[[Category: Stress-sensor]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Aug 25 08~~:56:45 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:55:17 2010''

OCA at 04:48, 25 August 2010

OCA — Wed, 25 Aug 2010 04:48:58 GMT

←Older revision		Revision as of 04:48, 25 August 2010
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3lgi.jpg\|left\|200px]]

-	The ~~entry 3lgi~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3lgi", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3lgi\| PDB=3lgi \| SCENE= }}

-	~~Authors: Sohn, J., Grant, R~~.A~~.., Sauer, R.T.~~	+	===Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A===

-	Description: Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Feb 17 10~~:10:20 2010''	+	==About this Structure==
		+	3LGI is a 3 chains structure with sequences 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=3LGI OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Grant, R A..]]
		+	[[Category: Sauer, R T.]]
		+	[[Category: Sohn, J.]]
		+	[[Category: Htra]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pdz omp]]
		+	[[Category: Protease]]
		+	[[Category: Serine protease]]
		+	[[Category: Stress-sensor]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:56:45 2010''

OCA at 08:10, 17 February 2010

OCA — Wed, 17 Feb 2010 08:10:20 GMT

←Older revision		Revision as of 08:10, 17 February 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3lgi is ON HOLD	+	The entry 3lgi is ON HOLD until Paper Publication

	Authors: Sohn, J., Grant, R.A.., Sauer, R.T.		Authors: Sohn, J., Grant, R.A.., Sauer, R.T.
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	Description: Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A		Description: Structure of the protease domain of DegS (DegS-deltaPDZ) at 1.65 A

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 16:58:29 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 10:10:20 2010''