1a0f - Revision history

OCA at 06:26, 7 February 2024

2024-02-07T06:26:36Z

←Older revision		Revision as of 06:26, 7 February 2024
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	<StructureSection load='1a0f' size='340' side='right'caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1a0f' size='340' side='right'caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a0f]] is a 2 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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1A0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a0f]] is a 2 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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0F FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</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]] 2.1Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~83333 ECOLI])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]~~ </~~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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [https://pdbe.org/1a0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [https://www.ebi.ac.uk/pdbsum/1a0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [~~http~~://pdbe.org/1a0f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1a0f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0f ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GSTA_ECOLI GSTA_ECOLI]] Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:7798255</ref> <ref>PMID:2185038</ref> <ref>PMID:17018556</ref> <ref>PMID:18778244</ref>	+	[https://www.uniprot.org/uniprot/GSTA_ECOLI GSTA_ECOLI] Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:7798255</ref> <ref>PMID:2185038</ref> <ref>PMID:17018556</ref> <ref>PMID:18778244</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1a0f 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=1a0f ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Cytosolic glutathione S-transferase is a family of multi-functional enzymes involved in the detoxification of a large variety of xenobiotic and endobiotic compounds through glutathione conjugation. The three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate, N-(N-L-gamma-glutamyl-3-sulfo-L-alanyl)-glycine, has been determined by the multiple isomorphous replacement method and refined to a crystallographic R factor of 0.183 at 2.1 A resolution. The E. coli enzyme is a globular homodimer with dimensions of 58 Ax56 Ax52 A. Each subunit, consisting of a polypeptide of 201 amino acid residues, is divided into a smaller N-terminal domain (residues 1 to 80) and a larger C-terminal one (residues 89 to 201). The core of the N-terminal domain is constructed by a four-stranded beta-sheet and two alpha-helices, and that of the C-terminal one is constructed by a right-handed bundle of four alpha-helices. Glutathione sulfonate, a competitive inhibitor against glutathione, is bound in a cleft between the N and C-terminal domains. Therefore, the E. coli enzyme conserves overall constructions common to the eukaryotic enzymes, in its polypeptide fold, dimeric assembly, and glutathione-binding site. In the case of the eukaryotic enzymes, tyrosine and serine residues near the N terminus are located in the proximity of the sulfur atom of the bound glutathione, and are proposed to be catalytically essential. In the E. coli enzyme, Tyr5 and Ser11 corresponding to these residues are not involved in the interaction with the inhibitor, although they are located in the vicinity of catalytic site. Instead, Cys10 N and His106 Nepsilon2 atoms are hydrogen-bonded to the sulfonate group of the inhibitor. On the basis of this structural study, Cys10 and His106 are ascribed to the catalytic residues that are distinctive from the family of the eukaryotic enzymes. We propose that glutathione S-transferases have diverged from a common origin and acquired different catalytic apparatuses in the process of evolution.
-
-	Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106.,Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K J Mol Biol. 1998 Aug 7;281(1):135-47. PMID:9680481<ref>PMID:9680481</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1a0f" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli]]~~	+	[[Category: Escherichia coli K-12]]
-	~~[[Category: Glutathione transferase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Harada, S]]	+	[[Category: Harada S]]
-	[[Category: Inoue, H]]	+	[[Category: Inoue H]]
-	[[Category: Nishida, M]]	+	[[Category: Nishida M]]
-	[[Category: Noguchi, S]]	+	[[Category: Noguchi S]]
-	[[Category: Satow, Y]]	+	[[Category: Satow Y]]
-	[[Category: Takahashi, K]]	+	[[Category: Takahashi K]]
-	~~[[Category: Detoxification]]~~	+
-	~~[[Category: Glutahione conjugation]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:06, 18 November 2020

2020-11-18T10:06:53Z

←Older revision		Revision as of 10:06, 18 November 2020
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	==CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID==		==CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID==
-	<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1a0f' size='340' side='right'caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a0f]] is a 2 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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1A0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a0f]] is a 2 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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1A0F FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://pdbe.org/1a0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://pdbe.org/1a0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/1a0f_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/1a0f_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>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1a0f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1a0f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Ecoli]]		[[Category: Ecoli]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
		+	[[Category: Large Structures]]
	[[Category: Harada, S]]		[[Category: Harada, S]]
	[[Category: Inoue, H]]		[[Category: Inoue, H]]

OCA at 10:47, 8 November 2017

2017-11-08T10:47:35Z

←Older revision		Revision as of 10:47, 8 November 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID==		==CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID==
	<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://pdbe.org/1a0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://pdbe.org/1a0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1a0f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1a0f" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:25, 7 February 2016

2016-02-07T15:25:56Z

←Older revision		Revision as of 15:25, 7 February 2016
Line 18:		Line 18:
	<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=1a0f ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:51, 9 September 2015

2015-09-09T15:51:05Z

←Older revision		Revision as of 15:51, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a0f]] is a 2 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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0F FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://pdbe.org/1a0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1a0f" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Harada, S]]		[[Category: Harada, S]]

OCA at 16:16, 24 December 2014

2014-12-24T16:16:46Z

←Older revision		Revision as of 16:16, 24 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSTA_ECOLI GSTA_ECOLI]] Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.<ref>PMID:7798255</ref> <ref>PMID:2185038</ref> <ref>PMID:17018556</ref> <ref>PMID:18778244</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:05, 22 December 2014

2014-12-22T11:05:45Z

←Older revision		Revision as of 11:05, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0F FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0F FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f 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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
-	[[Category: Harada, S.]]	+	[[Category: Harada, S]]
-	[[Category: Inoue, H.]]	+	[[Category: Inoue, H]]
-	[[Category: Nishida, M.]]	+	[[Category: Nishida, M]]
-	[[Category: Noguchi, S.]]	+	[[Category: Noguchi, S]]
-	[[Category: Satow, Y.]]	+	[[Category: Satow, Y]]
-	[[Category: Takahashi, K.]]	+	[[Category: Takahashi, K]]
	[[Category: Detoxification]]		[[Category: Detoxification]]
	[[Category: Glutahione conjugation]]		[[Category: Glutahione conjugation]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:30, 23 July 2014

2014-07-23T08:30:42Z

←Older revision		Revision as of 08:30, 23 July 2014
Line 1:		Line 1:
-	[[~~Image:~~1a0f.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID==
		+	<StructureSection load='1a0f' size='340' side='right' caption='[[1a0f]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A0F FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1a0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a0f RCSB], [http://www.ebi.ac.uk/pdbsum/1a0f 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/a0/1a0f_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 ==
		+	Cytosolic glutathione S-transferase is a family of multi-functional enzymes involved in the detoxification of a large variety of xenobiotic and endobiotic compounds through glutathione conjugation. The three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate, N-(N-L-gamma-glutamyl-3-sulfo-L-alanyl)-glycine, has been determined by the multiple isomorphous replacement method and refined to a crystallographic R factor of 0.183 at 2.1 A resolution. The E. coli enzyme is a globular homodimer with dimensions of 58 Ax56 Ax52 A. Each subunit, consisting of a polypeptide of 201 amino acid residues, is divided into a smaller N-terminal domain (residues 1 to 80) and a larger C-terminal one (residues 89 to 201). The core of the N-terminal domain is constructed by a four-stranded beta-sheet and two alpha-helices, and that of the C-terminal one is constructed by a right-handed bundle of four alpha-helices. Glutathione sulfonate, a competitive inhibitor against glutathione, is bound in a cleft between the N and C-terminal domains. Therefore, the E. coli enzyme conserves overall constructions common to the eukaryotic enzymes, in its polypeptide fold, dimeric assembly, and glutathione-binding site. In the case of the eukaryotic enzymes, tyrosine and serine residues near the N terminus are located in the proximity of the sulfur atom of the bound glutathione, and are proposed to be catalytically essential. In the E. coli enzyme, Tyr5 and Ser11 corresponding to these residues are not involved in the interaction with the inhibitor, although they are located in the vicinity of catalytic site. Instead, Cys10 N and His106 Nepsilon2 atoms are hydrogen-bonded to the sulfonate group of the inhibitor. On the basis of this structural study, Cys10 and His106 are ascribed to the catalytic residues that are distinctive from the family of the eukaryotic enzymes. We propose that glutathione S-transferases have diverged from a common origin and acquired different catalytic apparatuses in the process of evolution.

-	~~{{STRUCTURE_1a0f\| PDB=1a0f \| SCENE= }}~~	+	Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106.,Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K J Mol Biol. 1998 Aug 7;281(1):135-47. PMID:9680481<ref>PMID:9680481</ref>

-	~~===CRYSTAL STRUCTURE OF GLUTATHIONE~~ S~~-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_9680481}}~~	+	==See Also==
-		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA~~].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:009680481<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]

OCA: Protected "1a0f" [edit=sysop:move=sysop]

2012-10-21T11:49:15Z

Protected "1a0f" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:49, 21 October 2012

OCA at 11:49, 21 October 2012

2012-10-21T11:49:11Z

←Older revision		Revision as of 11:49, 21 October 2012
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-	{{Seed}}
	[[Image:1a0f.png\|left\|200px]]		[[Image:1a0f.png\|left\|200px]]

-	<!--
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-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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	{{STRUCTURE_1a0f\| PDB=1a0f \| SCENE= }}		{{STRUCTURE_1a0f\| PDB=1a0f \| SCENE= }}

	===CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID===		===CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9680481}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9680481 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_9680481}}		{{ABSTRACT_PUBMED_9680481}}

	==About this Structure==		==About this Structure==
-	~~1A0F~~ is a 2 ~~chains~~ structure ~~of 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=1A0F OCA].	+	[[1a0f]] is a 2 chain structure with sequence from [http://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=1A0F OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9680481~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009680481</ref><references group="xtra"/>
-	[[Category: Escherichia coli]]	+	[[Category: Escherichia coli k-12]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Harada, S.]]		[[Category: Harada, S.]]
Line 35:		Line 23:
	[[Category: Glutahione conjugation]]		[[Category: Glutahione conjugation]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:46:12 2009''