5lcz - Revision history

OCA at 08:56, 11 October 2023

2023-10-11T08:56:31Z

←Older revision		Revision as of 08:56, 11 October 2023
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	<StructureSection load='5lcz' size='340' side='right'caption='[[5lcz]], [[Resolution\|resolution]] 2.33Å' scene=''>		<StructureSection load='5lcz' size='340' side='right'caption='[[5lcz]], [[Resolution\|resolution]] 2.33Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lcz]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lcz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LCZ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=GSH:GLUTATHIONE'>GSH</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]] 2.325Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~GSTA1 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></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=5lcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcz OCA], [~~http~~://pdbe.org/5lcz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lcz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lcz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcz 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=5lcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcz OCA], [https://pdbe.org/5lcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lcz RCSB], [https://www.ebi.ac.uk/pdbsum/5lcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>	+	[https://www.uniprot.org/uniprot/GSTA2_RAT GSTA2_RAT] Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.[UniProtKB:P10648][https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Axarli, A~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Chronopoulou, E G]]~~	+	[[Category: Axarli A]]
-	~~[[Category: Labrou, N E]]~~	+	[[Category: Chronopoulou EG]]
-	~~[[Category: Muleta,~~ A W]]	+	[[Category: Labrou NE]]
-	[[Category: ~~Papageorgiou, A C~~]]	+	[[Category: Muleta AW]]
-	[[Category: ~~Directed evolution~~]]	+	[[Category: Papageorgiou AC]]
-	[[Category: ~~Glutathione transferase a1-1~~]]	+
-	[[Category: ~~Protein stability]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 12:24, 17 July 2019

2019-07-17T12:24:38Z

←Older revision		Revision as of 12:24, 17 July 2019
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	==Chimeric GST==		==Chimeric GST==
-	<StructureSection load='5lcz' size='340' side='right' caption='[[5lcz]], [[Resolution\|resolution]] 2.33Å' scene=''>	+	<StructureSection load='5lcz' size='340' side='right'caption='[[5lcz]], [[Resolution\|resolution]] 2.33Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lcz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LCZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lcz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LCZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5lcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcz OCA], [http://pdbe.org/5lcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcz RCSB], [http://www.ebi.ac.uk/pdbsum/5lcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcz 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=5lcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcz OCA], [http://pdbe.org/5lcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcz RCSB], [http://www.ebi.ac.uk/pdbsum/5lcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcz ProSAT]</span></td></tr>
	</table>		</table>
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	</div>		</div>
	<div class="pdbe-citations 5lcz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5lcz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Axarli, A]]		[[Category: Axarli, A]]
	[[Category: Chronopoulou, E G]]		[[Category: Chronopoulou, E G]]

OCA at 13:59, 21 September 2016

2016-09-21T13:59:09Z

←Older revision		Revision as of 13:59, 21 September 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lcz is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Chimeric GST==
		+	<StructureSection load='5lcz' size='340' side='right' caption='[[5lcz]], [[Resolution\|resolution]] 2.33Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5lcz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LCZ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></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=5lcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcz OCA], [http://pdbe.org/5lcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lcz RCSB], [http://www.ebi.ac.uk/pdbsum/5lcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcz ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: Glutathione transferases (GSTs) are a family of detoxification enzymes that catalyse the conjugation of glutathione (GSH) to electrophilic compounds. METHODS: A library of alpha class GSTs was constructed by DNA shuffling using the DNA encoding the human glutathione transferase A1-1 (hGSTA1-1) and the rat glutathione transferase A1-1 (rGSTA1-1). RESULTS: Activity screening of the library allowed the selection of a chimeric enzyme variant (GSTD4) that displayed high affinity towards GSH and GSH-Sepharose affinity adsorbent, higher kcat/Km and improved thermal stability, compared to the parent enzymes. The crystal structures of the GSTD4 enzyme in free form and in complex with GSH were determined to 1.6A and 2.3A resolution, respectively. Analysis of the GSTD4 structure showed subtle conformational changes in the GSH-binding site and in electron-sharing network that may contribute to the increased GSH affinity. The shuffled variant GSTD4 was further optimised for improved oxidative stability employing site-saturation mutagenesis. The Cys112Ser mutation confers optimal oxidative stability and kinetic properties in the GSTD4 enzyme. CONCLUSIONS: DNA shuffling allowed the creation of a chimeric enzyme variant with improved properties, compared to the parent enzymes. X-ray crystallography shed light on how recombination of a specific segments from homologous GSTA1-1 together with point mutations gives rise to a new functionally competent enzyme with improved binding, catalytic properties and stability. GENERAL SIGNIFICANCE: Such an engineered GST would be useful in biotechnology as affinity tool in affinity chromatography as well as a biocatalytic matrix for the construction of biochips or enzyme biosensors.

-	~~Authors: Axarli, A~~., Muleta~~, A.W.~~, Chronopoulou~~, E.G.~~, Papageorgiou, A.C., ~~Labrou, N~~.E.	+	Directed Evolution of Glutathione Transferases Towards a Selective Glutathione-Binding Site and Improved Oxidative Stability.,Axarli I, Muleta AW, Chronopoulou EG, Papageorgiou AC, Labrou NE Biochim Biophys Acta. 2016 Sep 6. pii: S0304-4165(16)30326-9. doi:, 10.1016/j.bbagen.2016.09.004. PMID:27612661<ref>PMID:27612661</ref>

-	~~Description: Chimeric GST~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category: Chronopoulou~~, E.~~G]]~~	+	<div class="pdbe-citations 5lcz" style="background-color:#fffaf0;"></div>
-	~~[[Category: Labrou, N~~.~~E]]~~	+	== References ==
-	~~[[Category~~: ~~Papageorgiou, A.C]]~~	+	<references/>
-	~~[[Category: Muleta, A.W]]~~	+	__TOC__
		+	</StructureSection>
	[[Category: Axarli, A]]		[[Category: Axarli, A]]
		+	[[Category: Chronopoulou, E G]]
		+	[[Category: Labrou, N E]]
		+	[[Category: Muleta, A W]]
		+	[[Category: Papageorgiou, A C]]
		+	[[Category: Directed evolution]]
		+	[[Category: Glutathione transferase a1-1]]
		+	[[Category: Protein stability]]
		+	[[Category: Transferase]]

OCA at 02:39, 4 August 2016

2016-08-04T02:39:13Z

←Older revision		Revision as of 02:39, 4 August 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5lcz is ON HOLD	+	The entry 5lcz is ON HOLD until Paper Publication

	Authors: Axarli, A., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E.		Authors: Axarli, A., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E.

OCA: Protected "5lcz" [edit=sysop:move=sysop]

2016-07-13T00:59:41Z

Protected "5lcz" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:59, 13 July 2016

OCA: New page: '''Unreleased structure''' The entry 5lcz is ON HOLD Authors: Axarli, A., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E. Description: Chimeric GST [[Category: Unrel...

2016-07-13T00:59:40Z

New page: '''Unreleased structure''' The entry 5lcz is ON HOLD Authors: Axarli, A., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E. Description: Chimeric GST [[Category: Unrel...

New page

'''Unreleased structure'''

The entry 5lcz is ON HOLD

Authors: Axarli, A., Muleta, A.W., Chronopoulou, E.G., Papageorgiou, A.C., Labrou, N.E.

Description: Chimeric GST
[[Category: Unreleased Structures]]
[[Category: Chronopoulou, E.G]]
[[Category: Labrou, N.E]]
[[Category: Papageorgiou, A.C]]
[[Category: Muleta, A.W]]
[[Category: Axarli, A]]