2v6k - Revision history

OCA at 15:08, 13 December 2023

OCA — Wed, 13 Dec 2023 15:08:03 GMT

←Older revision		Revision as of 15:08, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2v6k' size='340' side='right'caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='2v6k' size='340' side='right'caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Pseudomonas_sp~~.~~_u2 Pseudomonas~~ sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ralstonia_sp._U2 Ralstonia sp. U2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</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]] 1.3Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [https://pdbe.org/2v6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [https://www.ebi.ac.uk/pdbsum/2v6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6k 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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [https://pdbe.org/2v6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [https://www.ebi.ac.uk/pdbsum/2v6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6k ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/NAGL_RALSP NAGL_RALSP] Catalyzes the GSH-dependent isomerization of maleylpyruvate to fumarylpyruvate which is subsequently processed by NagK to form pyruvate and fumarate.<ref>PMID:11133965</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 2v6k" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2v6k" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Maleylacetoacetate isomerase]]~~	+	[[Category: Ralstonia sp. U2]]
-	~~[[Category: Pseudomonas~~ sp. u2]]	+	[[Category: Hadfield AT]]
-	[[Category: Hadfield~~, A T~~]]	+	[[Category: Shoemark DK]]
-	[[Category: Shoemark~~, D K~~]]	+	[[Category: Williams PA]]
-	[[Category: Williams~~, P A~~]]	+	[[Category: Zhou N-Y]]
-	[[Category: Zhou, N Y]]	+
-	~~[[Category: Bacterial]]~~	+
-	~~[[Category: Biodegradation]]~~	+
-	~~[[Category: Fumaryl pyruvate]]~~	+
-	~~[[Category: Glutathione-s-transferase]]~~	+
-	~~[[Category: Gst]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Maleyl pyruvate]]~~	+
-	~~[[Category: Plasmid]]~~	+
-	~~[[Category: Pyruvate~~]]	+

OCA at 20:58, 20 October 2021

OCA — Wed, 20 Oct 2021 20:58:19 GMT

←Older revision		Revision as of 20:58, 20 October 2021
Line 3:		Line 3:
	<StructureSection load='2v6k' size='340' side='right'caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='2v6k' size='340' side='right'caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Pseudomonas_sp._u2 Pseudomonas sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2V6K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._u2 Pseudomonas sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [~~http~~://pdbe.org/2v6k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2v6k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6k 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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [https://pdbe.org/2v6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [https://www.ebi.ac.uk/pdbsum/2v6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6k ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 14:18, 18 December 2019

OCA — Wed, 18 Dec 2019 14:18:42 GMT

←Older revision		Revision as of 14:18, 18 December 2019
Line 1:		Line 1:

	==Structure of Maleyl Pyruvate Isomerase, a bacterial glutathione-s- transferase in Zeta class, in complex with substrate analogue dicarboxyethyl glutathione==		==Structure of Maleyl Pyruvate Isomerase, a bacterial glutathione-s- transferase in Zeta class, in complex with substrate analogue dicarboxyethyl glutathione==
-	<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>	+	<StructureSection load='2v6k' size='340' side='right'caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._u2 Pseudomonas sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>		<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._u2 Pseudomonas sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
Line 31:		Line 31:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
	[[Category: Pseudomonas sp. u2]]		[[Category: Pseudomonas sp. u2]]

OCA at 19:02, 24 January 2018

OCA — Wed, 24 Jan 2018 19:02:43 GMT

←Older revision		Revision as of 19:02, 24 January 2018
Line 1:		Line 1:
-	==~~STRUCTURE OF MALEYL PYRUVATE ISOMERASE~~, ~~A BACTERIAL GLUTATHIONE~~-S-~~TRANSFERASE IN ZETA CLASS~~, ~~IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE~~==	+
		+	==Structure of Maleyl Pyruvate Isomerase, a bacterial glutathione-s- transferase in Zeta class, in complex with substrate analogue dicarboxyethyl glutathione==
	<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://pdbe.org/2v6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k 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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://pdbe.org/2v6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6k ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v6k_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v6k_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 43:		Line 44:
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Maleyl pyruvate]]		[[Category: Maleyl pyruvate]]
		+	[[Category: Plasmid]]
	[[Category: Pyruvate]]		[[Category: Pyruvate]]

OCA at 13:44, 7 February 2016

OCA — Sun, 07 Feb 2016 13:44:31 GMT

←Older revision		Revision as of 13:44, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ralstonia_sp~~. ~~Ralstonia~~ sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._u2 Pseudomonas sp. u2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k 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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://pdbe.org/2v6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 15:		Line 15:
	<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=2v6k ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 25:		Line 25:
	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 2v6k" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
-	[[Category: ~~Ralstonia~~ sp]]	+	[[Category: Pseudomonas sp. u2]]
	[[Category: Hadfield, A T]]		[[Category: Hadfield, A T]]
	[[Category: Shoemark, D K]]		[[Category: Shoemark, D K]]

OCA at 15:53, 19 January 2015

OCA — Mon, 19 Jan 2015 15:53:33 GMT

←Older revision		Revision as of 15:53, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_sp. Ralstonia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>		<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_sp. Ralstonia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k 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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k 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 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
-	[[Category: Ralstonia sp.]]	+	[[Category: Ralstonia sp]]
-	[[Category: Hadfield, A T.]]	+	[[Category: Hadfield, A T]]
-	[[Category: Shoemark, D K.]]	+	[[Category: Shoemark, D K]]
-	[[Category: Williams, P A.]]	+	[[Category: Williams, P A]]
-	[[Category: Zhou, N Y.]]	+	[[Category: Zhou, N Y]]
	[[Category: Bacterial]]		[[Category: Bacterial]]
	[[Category: Biodegradation]]		[[Category: Biodegradation]]

OCA at 02:14, 1 October 2014

OCA — Wed, 01 Oct 2014 02:14:33 GMT

←Older revision		Revision as of 02:14, 1 October 2014
Line 1:		Line 1:
-	[[~~Image~~:2v6k.~~png\|left~~\|200px]]	+	==STRUCTURE OF MALEYL PYRUVATE ISOMERASE, A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE==
		+	<StructureSection load='2v6k' size='340' side='right' caption='[[2v6k]], [[Resolution\|resolution]] 1.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_sp. Ralstonia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6K FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TGG:GAMMA-GLUTAMYL-S-(1,2-DICARBOXYETHYL)CYSTEINYLGLYCINE'>TGG</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maleylacetoacetate_isomerase Maleylacetoacetate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.2 5.2.1.2] </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=2v6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v6k RCSB], [http://www.ebi.ac.uk/pdbsum/2v6k 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/v6/2v6k_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 ==
		+	Maleyl pyruvate isomerase (MPI) is a bacterial glutathione S-transferase (GST) from the pathway for degradation of naphthalene via gentisate that enables the bacterium Ralstonia to use polyaromatic hydrocarbons as a sole carbon source. Genome sequencing projects have revealed the presence of large numbers of GSTs in bacterial genomes, often located within gene clusters encoding the degradation of different aromatic compounds. This structure is therefore an example of this under-represented class of enzymes. Unlike many glutathione transferases, the reaction catalysed by MPI is an isomerisation of an aromatic ring breakdown product, and glutathione is a true cofactor rather than a substrate in the reaction. We have solved the structure of the enzyme in complex with dicarboxyethyl glutathione, an analogue of a proposed reaction intermediate, at a resolution of 1.3 A. The structure provides direct evidence that the glutathione thiolate attacks the substrate in the C2 position, with the terminal carboxylate buried at the base of the active site cleft. Our structures suggest that the C1-C2 bond remains fixed so when rotation occurs around the C2-C3 bond the atoms from C4 onwards actually move. We identified a conserved arginine that is likely to stabilize the enolate form of the substrate during the isomerisation. Arginines at either side of the active site cleft can interact with the end of the substrate/product and preferentially stabilise the product. MPI has significant sequence similarity to maleylacetoacetate isomerase (MAAI), which performs an analogous reaction in the catabolism of phenylalanine and tyrosine. The proposed mechanism therefore has relevance to the MAAIs. Significantly, whilst the overall sequence identity is 40% only one of the five residues from the Zeta motif in the active site is conserved. We re-examined the roles of the residues in the active site of both enzymes and the Zeta motif itself.

-	~~{{STRUCTURE_2v6k\| PDB=2v6k \| SCENE= }}~~	+	Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation.,Marsh M, Shoemark DK, Jacob A, Robinson C, Cahill B, Zhou NY, Williams PA, Hadfield AT J Mol Biol. 2008 Dec 5;384(1):165-77. Epub 2008 Sep 19. PMID:18824004<ref>PMID:18824004</ref>

-	~~===STRUCTURE OF MALEYL PYRUVATE ISOMERASE~~, ~~A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18824004}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2v6k]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Ralstonia_sp~~. ~~Ralstonia sp.]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:018824004<~~/~~ref~~><~~ref group="xtra">PMID:009573207</ref><references group="xtra"~~/>	+
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
	[[Category: Ralstonia sp.]]		[[Category: Ralstonia sp.]]

OCA at 13:12, 30 January 2013

OCA — Wed, 30 Jan 2013 13:12:15 GMT

←Older revision		Revision as of 13:12, 30 January 2013
Line 1:		Line 1:
	[[Image:2v6k.png\|left\|200px]]		[[Image:2v6k.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2v6k", 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_2v6k\| PDB=2v6k \| SCENE= }}		{{STRUCTURE_2v6k\| PDB=2v6k \| SCENE= }}

	===STRUCTURE OF MALEYL PYRUVATE ISOMERASE, A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE===		===STRUCTURE OF MALEYL PYRUVATE ISOMERASE, A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18824004}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18824004 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18824004}}		{{ABSTRACT_PUBMED_18824004}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18824004~~</ref><ref group="xtra">PMID:~~9573207~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018824004</ref><ref group="xtra">PMID:009573207</ref><references group="xtra"/>
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
	[[Category: Ralstonia sp.]]		[[Category: Ralstonia sp.]]
Line 36:		Line 25:
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Maleyl pyruvate]]		[[Category: Maleyl pyruvate]]
-	[[Category: Plasmid]]
	[[Category: Pyruvate]]		[[Category: Pyruvate]]

OCA: Protected "2v6k" [edit=sysop:move=sysop]

OCA — Mon, 14 Mar 2011 20:53:24 GMT

Protected "2v6k" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:53, 14 March 2011

OCA at 20:53, 14 March 2011

OCA — Mon, 14 Mar 2011 20:53:23 GMT

←Older revision		Revision as of 20:53, 14 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2v6k.png\|left\|200px]]		[[Image:2v6k.png\|left\|200px]]

Line 12:		Line 11:
	===STRUCTURE OF MALEYL PYRUVATE ISOMERASE, A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE===		===STRUCTURE OF MALEYL PYRUVATE ISOMERASE, A BACTERIAL GLUTATHIONE-S-TRANSFERASE IN ZETA CLASS, IN COMPLEX WITH SUBSTRATE ANALOGUE DICARBOXYETHYL GLUTATHIONE===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18824004}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18824004 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18824004}}

	==About this Structure==		==About this Structure==
-	~~2V6K~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Ralstonia_sp. Ralstonia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA].	+	[[2v6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_sp. Ralstonia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6K OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:9573207</ref><references group="xtra"/>	+	<ref group="xtra">PMID:18824004</ref><ref group="xtra">PMID:9573207</ref><references group="xtra"/>
	[[Category: Maleylacetoacetate isomerase]]		[[Category: Maleylacetoacetate isomerase]]
	[[Category: Ralstonia sp.]]		[[Category: Ralstonia sp.]]
Line 33:		Line 38:
	[[Category: Plasmid]]		[[Category: Plasmid]]
	[[Category: Pyruvate]]		[[Category: Pyruvate]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:11:59 2009''