4a9g - Revision history

OCA at 10:48, 9 May 2024

OCA — Thu, 09 May 2024 10:48:30 GMT

←Older revision		Revision as of 10:48, 9 May 2024
Line 3:		Line 3:
	<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>		<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a9g]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>~~[[4a8a\|4a8a]]~~, [[~~4a8b~~\|~~4a8b~~]]~~, [[4a8c\|4a8c]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 7.5Å</td></tr>
-	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en~~.~~wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [https://pdbe.org/4a9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [https://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [https://pdbe.org/4a9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [https://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref>	+	[https://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidase Do]]~~	+	[[Category: Canellas F]]
-	[[Category: Canellas, F]]	+	[[Category: Clausen T]]
-	[[Category: Clausen, T]]	+	[[Category: Ehrmann M]]
-	[[Category: Ehrmann, M]]	+	[[Category: Malet H]]
-	[[Category: Malet, H]]	+	[[Category: Saibil HR]]
-	[[Category: Saibil~~, H R~~]]	+	[[Category: Sawa J]]
-	[[Category: Sawa, J]]	+	[[Category: Thalassinos K]]
-	[[Category: Thalassinos, K]]	+	[[Category: Yan J]]
-	[[Category: Yan, J]]	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:53, 18 August 2022

OCA — Thu, 18 Aug 2022 07:53:57 GMT

←Older revision		Revision as of 07:53, 18 August 2022
Line 3:		Line 3:
	<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>		<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a9g]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [~~http~~://pdbe.org/4a9g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [https://pdbe.org/4a9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [https://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref>	+	[[https://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:48, 10 April 2020

OCA — Fri, 10 Apr 2020 18:48:16 GMT

←Older revision		Revision as of 18:48, 10 April 2020
Line 3:		Line 3:
	<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>		<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4A9G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://pdbe.org/4a9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://pdbe.org/4a9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:47, 6 March 2020

OCA — Fri, 06 Mar 2020 17:47:12 GMT

←Older revision		Revision as of 17:47, 6 March 2020
Line 1:		Line 1:

	==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==		==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
-	<~~StructureSection~~ load='4a9g' size='340' side='right'caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>	+	<SX load='4a9g' size='340' side='right' viewer='molstar' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
Line 22:		Line 22:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Ecoli]]		[[Category: Ecoli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 16:55, 28 August 2019

OCA — Wed, 28 Aug 2019 16:55:28 GMT

←Older revision		Revision as of 16:55, 28 August 2019
Line 1:		Line 1:

	==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==		==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
-	<StructureSection load='4a9g' size='340' side='right' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>	+	<StructureSection load='4a9g' size='340' side='right'caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Peptidase Do]]		[[Category: Peptidase Do]]
	[[Category: Canellas, F]]		[[Category: Canellas, F]]

OCA at 18:56, 4 August 2016

OCA — Thu, 04 Aug 2016 18:56:47 GMT

←Older revision		Revision as of 18:56, 4 August 2016
Line 1:		Line 1:
		+
	==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==		==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
	<StructureSection load='4a9g' size='340' side='right' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>		<StructureSection load='4a9g' size='340' side='right' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Hydrolase Hydrolase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g 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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://pdbe.org/4a9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4a9g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
-	[[Category: ~~Hydrolase~~]]	+	[[Category: Peptidase Do]]
	[[Category: Canellas, F]]		[[Category: Canellas, F]]
	[[Category: Clausen, T]]		[[Category: Clausen, T]]
Line 32:		Line 34:
	[[Category: Yan, J]]		[[Category: Yan, J]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
		+	[[Category: Hydrolase]]

OCA at 12:09, 25 December 2014

OCA — Thu, 25 Dec 2014 12:09:51 GMT

←Older revision		Revision as of 12:09, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g 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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DEGQ_ECOLI DEGQ_ECOLI]] DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.<ref>PMID:8576051</ref> <ref>PMID:8830688</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
-	[[Category: Canellas, F.]]	+	[[Category: Canellas, F]]
-	[[Category: Clausen, T.]]	+	[[Category: Clausen, T]]
-	[[Category: Ehrmann, M.]]	+	[[Category: Ehrmann, M]]
-	[[Category: Malet, H.]]	+	[[Category: Malet, H]]
-	[[Category: Saibil, H R.]]	+	[[Category: Saibil, H R]]
-	[[Category: Sawa, J.]]	+	[[Category: Sawa, J]]
-	[[Category: Thalassinos, K.]]	+	[[Category: Thalassinos, K]]
-	[[Category: Yan, J.]]	+	[[Category: Yan, J]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
-	[[Category: Hydrolase]]

OCA at 08:33, 5 June 2014

OCA — Thu, 05 Jun 2014 08:33:41 GMT

←Older revision		Revision as of 08:33, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~4a9g.~~png~~\|~~left~~\|~~200px~~]]	+	==Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein==
		+	<StructureSection load='4a9g' size='340' side='right' caption='[[4a9g]], [[Resolution\|resolution]] 7.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4a9g]] is a 24 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=4A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9G FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4a8a\|4a8a]], [[4a8b\|4a8b]], [[4a8c\|4a8c]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></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=4a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a9g RCSB], [http://www.ebi.ac.uk/pdbsum/4a9g PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function.

-	~~<!--~~	+	Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.,Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR Nat Struct Mol Biol. 2012 Jan 15;19(2):152-7. doi: 10.1038/nsmb.2210. PMID:22245966<ref>PMID:22245966</ref>
-	~~The line below this paragraph, containing "STRUCTURE_4a9g", 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_4a9g\| PDB=4a9g \| SCENE= }}~~	+

-	~~===Symmetrized cryo-EM reconstruction~~ of ~~E. coli DegQ 24-mer in complex with beta-casein===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22245966}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22245966 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22245966}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[4a9g]] is a 24 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=4A9G OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022245966<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 05:59, 15 February 2012

OCA — Wed, 15 Feb 2012 05:59:00 GMT

←Older revision		Revision as of 05:59, 15 February 2012
Line 11:		Line 11:
	===Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein===		===Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22245966}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22245966 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22245966}}

	==About this Structure==		==About this Structure==
	[[4a9g]] is a 24 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=4A9G OCA].		[[4a9g]] is a 24 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=4A9G OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022245966</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 06:31, 11 January 2012

OCA — Wed, 11 Jan 2012 06:31:02 GMT

←Older revision		Revision as of 06:31, 11 January 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4a9g.png\|left\|200px]]

-	The ~~entry 4a9g~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4a9g", 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_4a9g\| PDB=4a9g \| SCENE= }}

-	~~Authors: Malet, H., Canellas, F., Sawa, J., Yan, J., Thalassinos, K., Ehrmann, M., Clausen, T., Saibil, H.R~~.	+	===Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein===

-	~~Description~~: ~~Symmetrized cryo-EM reconstruction of E~~. coli ~~DegQ 24~~-~~mer in complex with beta-casein~~	+
		+	==About this Structure==
		+	[[4a9g]] is a 24 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=4A9G OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Hydrolase]]
		+	[[Category: Canellas, F.]]
		+	[[Category: Clausen, T.]]
		+	[[Category: Ehrmann, M.]]
		+	[[Category: Malet, H.]]
		+	[[Category: Saibil, H R.]]
		+	[[Category: Sawa, J.]]
		+	[[Category: Thalassinos, K.]]
		+	[[Category: Yan, J.]]
		+	[[Category: Chaperone]]
		+	[[Category: Hydrolase]]