1pkw - Revision history

OCA at 05:56, 17 April 2024

OCA — Wed, 17 Apr 2024 05:56:35 GMT

←Older revision		Revision as of 05:56, 17 April 2024
Line 3:		Line 3:
	<StructureSection load='1pkw' size='340' side='right'caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1pkw' size='340' side='right'caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKW FirstGlance]. <br>
-	</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>~~, ~~<scene name='pdbligand=HED:~~2~~-HYDROXYETHYL+DISULFIDE'>HED</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]] 2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td>~~<td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pkz\|1pkz]]~~, ~~[[1pl1\|1pl1]], [[1pl2\|1pl2]]~~<~~/div></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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [https://pdbe.org/1pkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [https://www.ebi.ac.uk/pdbsum/1pkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkw 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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [https://pdbe.org/1pkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [https://www.ebi.ac.uk/pdbsum/1pkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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>
	== 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=1pkw 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=1pkw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human glutathione transferase A1-1 is a well studied enzyme, but despite a wealth of structural and biochemical data a number of aspects of its catalytic function are still poorly understood. Here, five new crystal structures of this enzyme are described that provide several insights. Firstly, the structure of a complex of the wild-type human enzyme with glutathione was determined for the first time at 2.0 angstroms resolution. This reveals that glutathione binds in the G site in a very similar fashion as the glutathione portion of substrate analogues in other structures and also that glutathione binding alone is sufficient to stabilize the C-terminal helix of the protein. Secondly, we have studied the complex with a decarboxylated glutathione conjugate that is known to dramatically decrease the activity of the enzyme. The T68E mutant of human glutathione transferase A1-1 recovers some of the activity that is lost with the decarboxylated glutathione, but our structures of this mutant show that none of the earlier explanations of this phenomenon are likely to be correct. Thirdly, and serendipitously, the apo structures also reveal the conformation of the crucial C-terminal region that is disordered in all previous apo structures. The C-terminal region can adopt an ordered helix-like structure even in the apo state, but shows a strong tendency to unwind. Different conformations of the C-terminal regions were observed in the apo states of the two monomers, which suggests that cooperativity could play a role in the activity of the enzyme.
-
-	New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.,Grahn E, Novotny M, Jakobsson E, Gustafsson A, Grehn L, Olin B, Madsen D, Wahlberg M, Mannervik B, Kleywegt GJ Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):197-207. Epub 2006, Jan 18. PMID:16421451<ref>PMID:16421451</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1pkw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glutathione transferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Grahn, E]]	+	[[Category: Grahn E]]
-	[[Category: Grehn, L]]	+	[[Category: Grehn L]]
-	[[Category: Gustafsson, A]]	+	[[Category: Gustafsson A]]
-	[[Category: Jakobsson, E]]	+	[[Category: Jakobsson E]]
-	[[Category: Kleywegt~~, G J~~]]	+	[[Category: Kleywegt GJ]]
-	[[Category: Madsen, D]]	+	[[Category: Madsen D]]
-	[[Category: Mannervik, B]]	+	[[Category: Mannervik B]]
-	[[Category: Olin, B]]	+	[[Category: Olin B]]
-	[[Category: Wahlberg, M]]	+	[[Category: Wahlberg M]]
-	~~[[Category: Alpha-beta-domain]]~~	+
-	~~[[Category: Alpha-helical-domain]]~~	+
-	~~[[Category: Dimer]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:52, 15 September 2021

OCA — Wed, 15 Sep 2021 09:52:56 GMT

OCA at 19:03, 11 December 2019

OCA — Wed, 11 Dec 2019 19:03:59 GMT

←Older revision		Revision as of 19:03, 11 December 2019
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	==Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione==		==Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione==
-	<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1pkw' size='340' side='right'caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pkw]] 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=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pkw]] 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=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>
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: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Grahn, E]]		[[Category: Grahn, E]]
	[[Category: Grehn, L]]		[[Category: Grehn, L]]

OCA at 05:28, 8 March 2018

OCA — Thu, 08 Mar 2018 05:28:50 GMT

←Older revision		Revision as of 05:28, 8 March 2018
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1pkw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pkw" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:52, 24 February 2018

OCA — Sat, 24 Feb 2018 07:52:14 GMT

←Older revision		Revision as of 07:52, 24 February 2018
Line 1:		Line 1:
		+
	==Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione==		==Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione==
	<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://pdbe.org/1pkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw 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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://pdbe.org/1pkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkw 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/pk/1pkw_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/1pkw_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 31:
	</div>		</div>
	<div class="pdbe-citations 1pkw" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pkw" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:09, 8 February 2016

OCA — Mon, 08 Feb 2016 21:09:35 GMT

←Older revision		Revision as of 21:09, 8 February 2016
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=1pkw ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:24, 10 September 2015

OCA — Thu, 10 Sep 2015 15:24:55 GMT

←Older revision		Revision as of 15:24, 10 September 2015
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	<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pkw]] 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=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW 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>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</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>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw 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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://pdbe.org/1pkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw 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 1pkw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Grahn, E]]		[[Category: Grahn, E]]
	[[Category: Grehn, L]]		[[Category: Grehn, L]]

OCA at 02:10, 25 December 2014

OCA — Thu, 25 Dec 2014 02:10:11 GMT

←Older revision		Revision as of 02:10, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw 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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw PDBsum]</span></td></tr>
-	<table>	+	</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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Grahn, E.]]	+	[[Category: Grahn, E]]
-	[[Category: Grehn, L.]]	+	[[Category: Grehn, L]]
-	[[Category: Gustafsson, A.]]	+	[[Category: Gustafsson, A]]
-	[[Category: Jakobsson, E.]]	+	[[Category: Jakobsson, E]]
-	[[Category: Kleywegt, G J.]]	+	[[Category: Kleywegt, G J]]
-	[[Category: Madsen, D.]]	+	[[Category: Madsen, D]]
-	[[Category: Mannervik, B.]]	+	[[Category: Mannervik, B]]
-	[[Category: Olin, B.]]	+	[[Category: Olin, B]]
-	[[Category: Wahlberg, M.]]	+	[[Category: Wahlberg, M]]
	[[Category: Alpha-beta-domain]]		[[Category: Alpha-beta-domain]]
	[[Category: Alpha-helical-domain]]		[[Category: Alpha-helical-domain]]
	[[Category: Dimer]]		[[Category: Dimer]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 11:29, 3 October 2014

OCA — Fri, 03 Oct 2014 11:29:19 GMT

←Older revision		Revision as of 11:29, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1pkw\| PDB=1pkw \| SCENE= }}~~	+	==Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione==
-	===Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione===	+	<StructureSection load='1pkw' size='340' side='right' caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_16421451}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PKW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [http://www.ebi.ac.uk/pdbsum/1pkw 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/pk/1pkw_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 ==
		+	Human glutathione transferase A1-1 is a well studied enzyme, but despite a wealth of structural and biochemical data a number of aspects of its catalytic function are still poorly understood. Here, five new crystal structures of this enzyme are described that provide several insights. Firstly, the structure of a complex of the wild-type human enzyme with glutathione was determined for the first time at 2.0 angstroms resolution. This reveals that glutathione binds in the G site in a very similar fashion as the glutathione portion of substrate analogues in other structures and also that glutathione binding alone is sufficient to stabilize the C-terminal helix of the protein. Secondly, we have studied the complex with a decarboxylated glutathione conjugate that is known to dramatically decrease the activity of the enzyme. The T68E mutant of human glutathione transferase A1-1 recovers some of the activity that is lost with the decarboxylated glutathione, but our structures of this mutant show that none of the earlier explanations of this phenomenon are likely to be correct. Thirdly, and serendipitously, the apo structures also reveal the conformation of the crucial C-terminal region that is disordered in all previous apo structures. The C-terminal region can adopt an ordered helix-like structure even in the apo state, but shows a strong tendency to unwind. Different conformations of the C-terminal regions were observed in the apo states of the two monomers, which suggests that cooperativity could play a role in the activity of the enzyme.

-	~~==Function==~~	+	New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.,Grahn E, Novotny M, Jakobsson E, Gustafsson A, Grehn L, Olin B, Madsen D, Wahlberg M, Mannervik B, Kleywegt GJ Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):197-207. Epub 2006, Jan 18. PMID:16421451<ref>PMID:16421451</ref>
-	~~[[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1pkw]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Glutathione S-transferase\|Glutathione S-transferase]]		*[[Glutathione S-transferase\|Glutathione S-transferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:016421451</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 10:30, 16 April 2014

OCA — Wed, 16 Apr 2014 10:30:26 GMT

←Older revision		Revision as of 10:30, 16 April 2014
Line 1:		Line 1:
-	[[Image:1pkw.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_1pkw", 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_1pkw\| PDB=1pkw \| SCENE= }}		{{STRUCTURE_1pkw\| PDB=1pkw \| SCENE= }}
-
	===Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione===		===Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione===
		+	{{ABSTRACT_PUBMED_16421451}}

-		+	==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>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_16421451}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 16421451 is the PubMed ID~~ number.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_16421451}}~~	+

	==About this Structure==		==About this Structure==
	[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA].		[[1pkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA].
		+
		+	==See Also==
		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:016421451</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016421451</ref><references group="xtra"/><references/>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

←Older revision		Revision as of 09:52, 15 September 2021
Line 3:		Line 3:
	<StructureSection load='1pkw' size='340' side='right'caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1pkw' size='340' side='right'caption='[[1pkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pkw]] 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=1PKW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pkw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKW 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>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>	+	</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>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pkz\|1pkz]], [[1pl1\|1pl1]], [[1pl2\|1pl2]]</div></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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [~~http~~://pdbe.org/1pkw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1pkw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkw 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=1pkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkw OCA], [https://pdbe.org/1pkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkw RCSB], [https://www.ebi.ac.uk/pdbsum/1pkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkw 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/GSTA1_HUMAN GSTA1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]