1rov - Revision history

OCA at 08:25, 1 May 2024

OCA — Wed, 01 May 2024 08:25:53 GMT

←Older revision		Revision as of 08:25, 1 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROV FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROV FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</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=~~HLU~~:~~BETA-HYDROXYLEUCINE~~'>~~HLU~~</scene>, <scene name='pdbligand=~~HTR~~:BETA-~~HYDROXYTRYPTOPHANE~~'>~~HTR~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12]~~ </~~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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [https://pdbe.org/1rov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [https://www.ebi.ac.uk/pdbsum/1rov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rov 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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [https://pdbe.org/1rov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [https://www.ebi.ac.uk/pdbsum/1rov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rov ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.	+	[https://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</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=1rov 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=1rov ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Lipoxygenase catalysis depends in a critical fashion on the redox properties of a unique mononuclear non-heme iron cofactor. The isolated enzyme contains predominantly, if not exclusively, iron(II), but the catalytically active form of the enzyme has iron(III). The activating oxidation of the iron takes place in a reaction with the hydroperoxide product of the catalyzed reaction. In a second peroxide-dependent process, lipoxygenases are also inactivated. To examine the redox activation/inactivation dichotomy in lipoxygenase chemistry, the interaction between lipoxygenase-1 (and -3) and cumene hydroperoxide was investigated. Cumene hydroperoxide was a reversible inhibitor of the reaction catalyzed by lipoxygenase-1 under standard assay conditions at high substrate concentrations. Reconciliation of the data with the currently held kinetic mechanism requires simultaneous binding of substrate and peroxide. The enzyme also was both oxidized and largely inactivated in a reaction with the peroxide in the absence of substrate. The consequences of this reaction for the enzyme included the hydroxylation at C beta of two amino acid side chains in the vicinity of the cofactor, Trp and Leu. The modifications were identified by mass spectrometry and X-ray crystallography. The peroxide-induced oxidation of iron was also accompanied by a subtle rearrangement in the coordination sphere of the non-heme iron atom. Since the enzyme retains catalytic activity, albeit diminished, after treatment with cumene hydroperoxide, the structure of the iron site may reflect the catalytically relevant form of the cofactor.
-
-	Interaction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition.,Vahedi-Faridi A, Brault PA, Shah P, Kim YW, Dunham WR, Funk MO Jr J Am Chem Soc. 2004 Feb 25;126(7):2006-15. PMID:14971933<ref>PMID:14971933</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1rov" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Brault PA]]
-	[[Category: Brault~~, P A~~]]	+	[[Category: Dunham WR]]
-	[[Category: Dunham~~, W R~~]]	+	[[Category: Funk MO]]
-	[[Category: Funk~~, M O~~]]	+	[[Category: Kim YW]]
-	[[Category: Kim~~, Y W~~]]	+	[[Category: Shah P]]
-	[[Category: Shah, P]]	+	[[Category: Vahedi-Faridi A]]
-	[[Category: Vahedi-Faridi, A]]	+
-	~~[[Category: Beta hydroxylation~~]]	+

OCA at 07:19, 22 September 2021

OCA — Wed, 22 Sep 2021 07:19:41 GMT

←Older revision		Revision as of 07:19, 22 September 2021
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	<StructureSection load='1rov' size='340' side='right'caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1rov' size='340' side='right'caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ROV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [~~http~~://pdbe.org/1rov PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1rov PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1rov 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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [https://pdbe.org/1rov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [https://www.ebi.ac.uk/pdbsum/1rov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rov ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.	+	[[https://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:40, 11 December 2019

OCA — Wed, 11 Dec 2019 19:40:00 GMT

←Older revision		Revision as of 19:40, 11 December 2019
Line 1:		Line 1:

	==Lipoxygenase-3 Treated with Cumene Hydroperoxide==		==Lipoxygenase-3 Treated with Cumene Hydroperoxide==
-	<StructureSection load='1rov' size='340' side='right' caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1rov' size='340' side='right'caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROV FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROV FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Glycine max]]		[[Category: Glycine max]]
		+	[[Category: Large Structures]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Brault, P A]]		[[Category: Brault, P A]]

OCA at 07:10, 8 March 2018

OCA — Thu, 08 Mar 2018 07:10:43 GMT

←Older revision		Revision as of 07:10, 8 March 2018
Line 1:		Line 1:
		+
	==Lipoxygenase-3 Treated with Cumene Hydroperoxide==		==Lipoxygenase-3 Treated with Cumene Hydroperoxide==
	<StructureSection load='1rov' size='340' side='right' caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1rov' size='340' side='right' caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://pdbe.org/1rov PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov 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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://pdbe.org/1rov PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rov ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1rov_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1rov_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>
	</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=1rov ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:39, 11 September 2015

OCA — Fri, 11 Sep 2015 11:39:57 GMT

←Older revision		Revision as of 11:39, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Lipoxygenase Lipoxygenase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov 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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://pdbe.org/1rov PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1rov" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Glycine max]]		[[Category: Glycine max]]
-	[[Category: ~~Lipoxygenase~~]]	+	[[Category: Oxidoreductase]]
	[[Category: Brault, P A]]		[[Category: Brault, P A]]
	[[Category: Dunham, W R]]		[[Category: Dunham, W R]]
Line 41:		Line 42:
	[[Category: Vahedi-Faridi, A]]		[[Category: Vahedi-Faridi, A]]
	[[Category: Beta hydroxylation]]		[[Category: Beta hydroxylation]]
-	[[Category: Oxidoreductase]]

OCA at 15:57, 25 December 2014

OCA — Thu, 25 Dec 2014 15:57:55 GMT

←Older revision		Revision as of 15:57, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROV FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROV FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov 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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
-	[[Category: Brault, P A.]]	+	[[Category: Brault, P A]]
-	[[Category: Dunham, W R.]]	+	[[Category: Dunham, W R]]
-	[[Category: Funk, M O.]]	+	[[Category: Funk, M O]]
-	[[Category: Kim, Y W.]]	+	[[Category: Kim, Y W]]
-	[[Category: Shah, P.]]	+	[[Category: Shah, P]]
-	[[Category: Vahedi-Faridi, A.]]	+	[[Category: Vahedi-Faridi, A]]
	[[Category: Beta hydroxylation]]		[[Category: Beta hydroxylation]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 14:45, 29 September 2014

OCA — Mon, 29 Sep 2014 14:45:26 GMT

←Older revision		Revision as of 14:45, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1rov.~~png~~\|~~left~~\|200px]]	+	==Lipoxygenase-3 Treated with Cumene Hydroperoxide==
		+	<StructureSection load='1rov' size='340' side='right' caption='[[1rov]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROV FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLU:BETA-HYDROXYLEUCINE'>HLU</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1rov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rov RCSB], [http://www.ebi.ac.uk/pdbsum/1rov 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/ro/1rov_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 ==
		+	Lipoxygenase catalysis depends in a critical fashion on the redox properties of a unique mononuclear non-heme iron cofactor. The isolated enzyme contains predominantly, if not exclusively, iron(II), but the catalytically active form of the enzyme has iron(III). The activating oxidation of the iron takes place in a reaction with the hydroperoxide product of the catalyzed reaction. In a second peroxide-dependent process, lipoxygenases are also inactivated. To examine the redox activation/inactivation dichotomy in lipoxygenase chemistry, the interaction between lipoxygenase-1 (and -3) and cumene hydroperoxide was investigated. Cumene hydroperoxide was a reversible inhibitor of the reaction catalyzed by lipoxygenase-1 under standard assay conditions at high substrate concentrations. Reconciliation of the data with the currently held kinetic mechanism requires simultaneous binding of substrate and peroxide. The enzyme also was both oxidized and largely inactivated in a reaction with the peroxide in the absence of substrate. The consequences of this reaction for the enzyme included the hydroxylation at C beta of two amino acid side chains in the vicinity of the cofactor, Trp and Leu. The modifications were identified by mass spectrometry and X-ray crystallography. The peroxide-induced oxidation of iron was also accompanied by a subtle rearrangement in the coordination sphere of the non-heme iron atom. Since the enzyme retains catalytic activity, albeit diminished, after treatment with cumene hydroperoxide, the structure of the iron site may reflect the catalytically relevant form of the cofactor.

-	~~{{STRUCTURE_1rov\| PDB=1rov \| SCENE= }}~~	+	Interaction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition.,Vahedi-Faridi A, Brault PA, Shah P, Kim YW, Dunham WR, Funk MO Jr J Am Chem Soc. 2004 Feb 25;126(7):2006-15. PMID:14971933<ref>PMID:14971933</ref>

-	~~===Lipoxygenase-3 Treated with Cumene Hydroperoxide===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14971933}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1rov]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Glycine_max Glycine max]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:014971933<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]

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

OCA — Fri, 04 Jan 2013 10:45:06 GMT

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

←Older revision

Revision as of 10:45, 4 January 2013

OCA at 10:45, 4 January 2013

OCA — Fri, 04 Jan 2013 10:45:01 GMT

←Older revision		Revision as of 10:45, 4 January 2013
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-	{{Seed}}
	[[Image:1rov.png\|left\|200px]]		[[Image:1rov.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1rov", 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_1rov\| PDB=1rov \| SCENE= }}		{{STRUCTURE_1rov\| PDB=1rov \| SCENE= }}

	===Lipoxygenase-3 Treated with Cumene Hydroperoxide===		===Lipoxygenase-3 Treated with Cumene Hydroperoxide===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14971933}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14971933 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14971933}}		{{ABSTRACT_PUBMED_14971933}}

	==About this Structure==		==About this Structure==
-	~~1ROV~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA].	+	[[1rov]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14971933~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014971933</ref><references group="xtra"/>
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
Line 33:		Line 21:
	[[Category: Vahedi-Faridi, A.]]		[[Category: Vahedi-Faridi, A.]]
	[[Category: Beta hydroxylation]]		[[Category: Beta hydroxylation]]
-		+	[[Category: Oxidoreductase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 21:05:50 2009''~~	+

OCA at 19:05, 17 February 2009

OCA — Tue, 17 Feb 2009 19:05:51 GMT

←Older revision		Revision as of 19:05, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1ROV is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA].	+	1ROV is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROV OCA].

	==Reference==		==Reference==
-	Interaction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition., Vahedi-Faridi A, Brault PA, Shah P, Kim YW, Dunham WR, Funk MO Jr, J Am Chem Soc. 2004 Feb 25;126(7):2006-15. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/14971933 14971933]~~	+	<ref group="xtra">PMID:14971933</ref><references group="xtra"/>
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
-	[[Category: Single protein]]
	[[Category: Brault, P A.]]		[[Category: Brault, P A.]]
	[[Category: Dunham, W R.]]		[[Category: Dunham, W R.]]
Line 35:		Line 34:
	[[Category: Beta hydroxylation]]		[[Category: Beta hydroxylation]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue ~~Jul 29 05~~:08:~~15 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:05:50 2009''