4rr0 - Revision history

OCA at 12:54, 1 March 2024

2024-03-01T12:54:54Z

←Older revision		Revision as of 12:54, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<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>		<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='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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.054Å</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>
	== Function ==		== Function ==
	[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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS residues that cluster together at subunit-subunit interfaces in the trimer, link the active sites and substrate binding sites, and are crucial for stabilizing the active enzyme conformation in response to OMP signaling. These residues are conserved across the HtrA-protease family, including orthologs linked to human disease, supporting a common mechanism of allosteric activation. Indeed, mutation of residues at homologous positions in the DegP quality-control protease also eliminates allosteric activation.
-
-	A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases.,de Regt AK, Kim S, Sohn J, Grant RA, Baker TA, Sauer RT Structure. 2015 Mar 3;23(3):517-26. doi: 10.1016/j.str.2015.01.012. Epub 2015 Feb, 19. PMID:25703375<ref>PMID:25703375</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4rr0" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:25, 8 March 2023

2023-03-08T08:25:04Z

←Older revision		Revision as of 08:25, 8 March 2023
Line 3:		Line 3:
	<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 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>	+	<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='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>
-	<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>	+
	</table>		</table>
		+	== Function ==
		+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~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.	+	In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS residues that cluster together at subunit-subunit interfaces in the trimer, link the active sites and substrate binding sites, and are crucial for stabilizing the active enzyme conformation in response to OMP signaling. These residues are conserved across the HtrA-protease family, including orthologs linked to human disease, supporting a common mechanism of allosteric activation. Indeed, mutation of residues at homologous positions in the DegP quality-control protease also eliminates allosteric 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>	+	A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases.,de Regt AK, Kim S, Sohn J, Grant RA, Baker TA, Sauer RT Structure. 2015 Mar 3;23(3):517-26. doi: 10.1016/j.str.2015.01.012. Epub 2015 Feb, 19. PMID:25703375<ref>PMID:25703375</ref>

	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>
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Grant~~, R A~~]]	+	[[Category: Grant RA]]
-	[[Category: Sauer~~, R T]]~~	+	[[Category: Sauer RT]]
-	~~[[Category: Htra]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Pdz]]~~	+
-	~~[[Category: Protein quality control]]~~	+
-	~~[[Category: Stress response]]~~	+
-	~~[[Category: Upr~~]]	+

OCA at 10:36, 1 May 2019

2019-05-01T10:36:34Z

←Older revision		Revision as of 10:36, 1 May 2019
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]] 3.05Å' 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>
Line 20:		Line 21:
	__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]]

OCA at 17:32, 18 January 2017

2017-01-18T17:32:39Z

←Older revision		Revision as of 17:32, 18 January 2017
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]] 3.05Å' scene=''>		<StructureSection load='4rr0' size='340' side='right' caption='[[4rr0]], [[Resolution\|resolution]] 3.05Å' scene=''>
Line 4:		Line 5:
	<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. 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='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'>[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 14:		Line 15:
	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 4rr0" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:50, 11 March 2015

2015-03-11T11:50:55Z

←Older revision		Revision as of 11:50, 11 March 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==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=''>
		+	== 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>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1vcw\|1vcw]]</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>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~The entry 4rr0 is ON HOLD~~	+	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>

-	~~Authors: Sauer~~, R.T.~~, Grant, R.A~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: Sauer, R.T]]	+	__TOC__
-	[[Category: ~~Grant, R.A~~]]	+	</StructureSection>
		+	[[Category: Grant, R A]]
		+	[[Category: Sauer, R T]]
		+	[[Category: Htra]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pdz]]
		+	[[Category: Protein quality control]]
		+	[[Category: Stress response]]
		+	[[Category: Upr]]

OCA at 17:14, 24 December 2014

2014-12-24T17:14:37Z

←Older revision		Revision as of 17:14, 24 December 2014
Line 6:		Line 6:

	Description: re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE		Description: re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE
		+	[[Category: Unreleased Structures]]
		+	[[Category: Sauer, R.T]]
		+	[[Category: Grant, R.A]]

OCA: Protected "4rr0" [edit=sysop:move=sysop]

2014-11-19T11:30:59Z

Protected "4rr0" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:30, 19 November 2014

OCA: New page: '''Unreleased structure''' The entry 4rr0 is ON HOLD Authors: Sauer, R.T., Grant, R.A. Description: re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE

2014-11-19T11:30:58Z

New page: '''Unreleased structure''' The entry 4rr0 is ON HOLD Authors: Sauer, R.T., Grant, R.A. Description: re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE

New page

'''Unreleased structure'''

The entry 4rr0 is ON HOLD

Authors: Sauer, R.T., Grant, R.A.

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