3fyg - Revision history

OCA at 06:48, 9 August 2023

OCA — Wed, 09 Aug 2023 06:48:06 GMT

←Older revision		Revision as of 06:48, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='3fyg' size='340' side='right'caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3fyg' size='340' side='right'caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FYG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FYG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GPR:(9R,10R)~~-~~9-(S-GLUTATHIONYL)-10-HYDROXY-9~~,~~10-DIHYDROPHENANTHRENE'>GPR</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]] 2.2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~YOF~~:3-~~FLUOROTYROSINE~~'>~~YOF~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene>, <scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [https://pdbe.org/3fyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [https://www.ebi.ac.uk/pdbsum/3fyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyg 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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [https://pdbe.org/3fyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [https://www.ebi.ac.uk/pdbsum/3fyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.	+	[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
-	[[Category: Glutathione transferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Armstrong, R N~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Gilliland, G L~~]]	+	[[Category: Armstrong RN]]
-	[[Category: ~~Parsons, J F~~]]	+	[[Category: Gilliland GL]]
-	[[Category: ~~Xiao, G~~]]	+	[[Category: Parsons JF]]
-	[[Category: ~~3-fluorotyrosine]]~~	+	[[Category: Xiao G]]
-	~~[[Category: Detoxification enzyme]]~~	+
-	~~[[Category: Three-dimensional structure]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Unnatural amino acid~~]]	+

OCA at 15:47, 3 November 2021

OCA — Wed, 03 Nov 2021 15:47:12 GMT

←Older revision		Revision as of 15:47, 3 November 2021
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	==CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE==		==CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE==
-	<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='3fyg' size='340' side='right'caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FYG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FYG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [~~http~~://pdbe.org/3fyg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3fyg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyg 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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [https://pdbe.org/3fyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [https://www.ebi.ac.uk/pdbsum/3fyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.	+	[[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]	+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
		+	[[Category: Large Structures]]
	[[Category: Armstrong, R N]]		[[Category: Armstrong, R N]]
	[[Category: Gilliland, G L]]		[[Category: Gilliland, G L]]

OCA at 07:46, 5 December 2018

OCA — Wed, 05 Dec 2018 07:46:23 GMT

←Older revision		Revision as of 07:46, 5 December 2018
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE==		==CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE==
	<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://pdbe.org/3fyg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg 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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://pdbe.org/3fyg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/3fyg_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/3fyg_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 11:36, 8 February 2016

OCA — Mon, 08 Feb 2016 11:36:29 GMT

←Older revision		Revision as of 11:36, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FYG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FYG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg 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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://pdbe.org/3fyg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fyg ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3fyg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
-	[[Category: Rattus norvegicus]]
	[[Category: Armstrong, R N]]		[[Category: Armstrong, R N]]
	[[Category: Gilliland, G L]]		[[Category: Gilliland, G L]]

OCA at 23:01, 24 December 2014

OCA — Wed, 24 Dec 2014 23:01:58 GMT

←Older revision		Revision as of 23:01, 24 December 2014
Line 9:		Line 9:
	<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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg 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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:06, 3 December 2014

OCA — Wed, 03 Dec 2014 10:06:24 GMT

←Older revision		Revision as of 10:06, 3 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3fyg.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE==
		+	<StructureSection load='3fyg' size='340' side='right' caption='[[3fyg]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3fyg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FYG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YOF:3-FLUOROTYROSINE'>YOF</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=3fyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fyg RCSB], [http://www.ebi.ac.uk/pdbsum/3fyg 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/fy/3fyg_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 ==
		+	The structure of the tetradeca-(3-fluorotyrosyl) M1-1 GSH transferase (3-FTyr GSH transferase), a protein in which tyrosine residues are globally substituted by 3-fluorotyrosines has been determined at 2.2 A resolution. This variant was produced to study the effect on the enzymatic mechanism and the structure was undertaken to assess how the presence of the 3-fluorotyrosyl residue influences the protein conformation and hence its function. Although fluorinated amino acid residues have frequently been used in biochemical and NMR investigations of proteins, no structure of a protein that has been globally substituted with a fluorinated amino acid has previously been reported. Thus, this structure represents the first crystal structure of such a protein containing a library of 14 (28 crystallographically distinct) microenvironments from which the nature of the interactions of fluorine atoms with the rest of the protein can be evaluated. Numerous conformational changes are observed in the protein structure as a result of substitution of 3-fluorotyrosine for tyrosine. The results of the comparison of the crystal structure of the fluorinated protein with the native enzyme reveal that conformational changes are observed for most of the 3-fluorotyrosines. The largest differences are seen for residues where the fluorine, the OH, or both are directly involved in interactions with other regions of the protein or with a symmetry-related molecule. The fluorine atoms of the 3-fluorotyrosine interact primarily through hydrogen bonds with other residues and water molecules. In several cases, the conformation of a 3-fluorotyrosine is different in one of the monomers of the enzyme from that observed in the other, including different hydrogen-bonding patterns. Altered conformations can be related to differences in the crystal packing interactions of the two monomers in the asymmetric unit. The fluorine atom on the active-site Tyr6 is located near the S atom of the thioether product (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene and creates a different pattern of interactions between 3-fluorotyrosine 6 and the S atom. Studies of these interactions help explain why 3-FTyr GSH transferase exhibits spectral and kinetic properties distinct from the native GSH transferase.

-	~~{{STRUCTURE_3fyg\| PDB=3fyg \| SCENE= }}~~	+	Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine.,Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL J Mol Biol. 1998 Aug 14;281(2):323-39. PMID:9698551<ref>PMID:9698551</ref>

-	~~===CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9698551}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3fyg]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA].~~	+

	==See Also==		==See Also==
	*[[Glutathione S-transferase\|Glutathione S-transferase]]		*[[Glutathione S-transferase\|Glutathione S-transferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009698551<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Armstrong, R N.]]	+	[[Category: Armstrong, R N]]
-	[[Category: Gilliland, G L.]]	+	[[Category: Gilliland, G L]]
-	[[Category: Parsons, J F.]]	+	[[Category: Parsons, J F]]
-	[[Category: Xiao, G.]]	+	[[Category: Xiao, G]]
	[[Category: 3-fluorotyrosine]]		[[Category: 3-fluorotyrosine]]
	[[Category: Detoxification enzyme]]		[[Category: Detoxification enzyme]]

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

OCA — Wed, 20 Feb 2013 14:20:53 GMT

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

←Older revision

Revision as of 14:20, 20 February 2013

OCA at 14:20, 20 February 2013

OCA — Wed, 20 Feb 2013 14:20:49 GMT

←Older revision		Revision as of 14:20, 20 February 2013
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-	{{Seed}}
	[[Image:3fyg.png\|left\|200px]]		[[Image:3fyg.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3fyg", 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_3fyg\| PDB=3fyg \| SCENE= }}		{{STRUCTURE_3fyg\| PDB=3fyg \| SCENE= }}

	===CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE===		===CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9698551}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9698551 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9698551}}		{{ABSTRACT_PUBMED_9698551}}

	==About this Structure==		==About this Structure==
-	~~3FYG~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA].	+	[[3fyg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA].
		+
		+	==See Also==
		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9698551~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009698551</ref><references group="xtra"/>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 35:		Line 26:
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:42:06 2009''

OCA at 19:42, 16 February 2009

OCA — Mon, 16 Feb 2009 19:42:07 GMT

←Older revision		Revision as of 19:42, 16 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	3FYG is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA].	+	3FYG is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYG OCA].

	==Reference==		==Reference==
-	Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine., Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL, J Mol Biol. 1998 Aug 14;281(2):323-39. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9698551 9698551]~~	+	<ref group="xtra">PMID:9698551</ref><references group="xtra"/>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Single protein]]
	[[Category: Armstrong, R N.]]		[[Category: Armstrong, R N.]]
	[[Category: Gilliland, G L.]]		[[Category: Gilliland, G L.]]
Line 37:		Line 36:
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon ~~Jul 28 02~~:37:~~49 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:42:06 2009''

OCA at 23:37, 27 July 2008

OCA — Sun, 27 Jul 2008 23:37:53 GMT

←Older revision		Revision as of 23:37, 27 July 2008
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-	[[Image:3fyg.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:3fyg.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_3fyg\| PDB=3fyg \| SCENE= }}		{{STRUCTURE_3fyg\| PDB=3fyg \| SCENE= }}

-	~~'''~~CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE~~'''~~	+	===CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE===


-	~~==Overview==~~	+	<!--
-	The ~~structure of the tetradeca-(3-fluorotyrosyl) M1-1 GSH transferase (3-FTyr GSH transferase)~~, ~~a protein in which tyrosine residues are globally substituted by 3-fluorotyrosines has been determined at 2.2 A resolution. This variant was produced to study~~ the ~~effect on the enzymatic mechanism and the structure was undertaken~~ to ~~assess how~~ the presence of the 3-fluorotyrosyl residue influences the protein conformation and hence its function. Although fluorinated amino acid residues have frequently been used in biochemical and NMR investigations of proteins, no structure of a protein that has been globally substituted with a fluorinated amino acid has previously been reported. Thus, this structure represents the first crystal structure of such a protein containing a library of 14 (28 crystallographically distinct) microenvironments from which the nature of the interactions of fluorine atoms with the rest of the protein can be evaluated. Numerous conformational changes are observed in the protein structure as ~~a result of substitution of 3-fluorotyrosine for tyrosine~~. ~~The results of the comparison of the crystal structure of the fluorinated protein with the native enzyme reveal that conformational changes are observed for most of the 3-fluorotyrosines~~. ~~The largest differences are seen for residues~~ where the fluorine, the OH, or both are directly involved in interactions with other regions of the protein or with a symmetry-related molecule. The fluorine atoms of the 3-fluorotyrosine interact primarily through hydrogen bonds with other residues and water molecules. In several cases, the conformation of a 3-fluorotyrosine is ~~different in one of~~ the ~~monomers of the enzyme from that observed in the other, including different hydrogen-bonding patterns~~. ~~Altered conformations can be related to differences in the crystal packing interactions of the two monomers in the asymmetric unit. The fluorine atom on the active~~-~~site Tyr6 is located near the S atom of the thioether product (9R,10R)~~-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene and creates a different pattern of interactions between 3-fluorotyrosine 6 and the S atom. Studies of these interactions help explain why 3-FTyr GSH transferase exhibits spectral and kinetic properties distinct from the native GSH transferase.	+	The line below this paragraph, {{ABSTRACT_PUBMED_9698551}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 9698551 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_9698551}}

	==About this Structure==		==About this Structure==
Line 32:		Line 36:
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 22:~~02:10 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:37:49 2008''