2nvk - Revision history

OCA at 08:21, 30 October 2024

2024-10-30T08:21:45Z

← Older revision		Revision as of 08:21, 30 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvk_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvk_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 10:22, 30 August 2023

2023-08-30T10:22:49Z

← Older revision		Revision as of 10:22, 30 August 2023
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	<StructureSection load='2nvk' size='340' side='right'caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2nvk' size='340' side='right'caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Drome Drome~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NVK FirstGlance]. <br>		<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NVK FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</scene>~~, ~~<scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>Trxr-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~7227 DROME])</td~~><~~/tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Thioredoxin~~-~~disulfide_reductase Thioredoxin~~-~~disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9]~~ </~~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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [https://pdbe.org/2nvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [https://www.ebi.ac.uk/pdbsum/2nvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvk 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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [https://pdbe.org/2nvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [https://www.ebi.ac.uk/pdbsum/2nvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME]] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</ref>		[https://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Drome~~]]		[[Category: Drosophila melanogaster]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Thioredoxin-disulfide reductase]]~~		[[Category: Eckenroth BE]]
	[[Category: Eckenroth~~, B E~~]]		[[Category: Everse SJ]]
	[[Category: Everse~~, S J~~]]		[[Category: Hondal RJ]]
	[[Category: Hondal~~, R J~~]]		[[Category: Rould MA]]
	[[Category: Rould~~, M A]]~~
	~~[[Category: Flavoprotein]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Rossmann~~]]

OCA at 15:52, 8 June 2021

2021-06-08T15:52:12Z

← Older revision		Revision as of 15:52, 8 June 2021
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	==Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster==		==Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster==
	<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2nvk' size='340' side='right'caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2NVK FirstGlance]. <br>		<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NVK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [~~http~~://pdbe.org/2nvk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2nvk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvk 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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [https://pdbe.org/2nvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [https://www.ebi.ac.uk/pdbsum/2nvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME]] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</ref>		[[https://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME]] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvk_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvk_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>
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	==See Also==		==See Also==
	*[[~~User:Sarah Abdalla/~~Thioredoxin ~~Reductase~~\|~~User:Sarah Abdalla/~~Thioredoxin ~~Reductase~~]]		*[[Thioredoxin reductase 3D structures\|Thioredoxin reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Drome]]		[[Category: Drome]]
			[[Category: Large Structures]]
	[[Category: Thioredoxin-disulfide reductase]]		[[Category: Thioredoxin-disulfide reductase]]
	[[Category: Eckenroth, B E]]		[[Category: Eckenroth, B E]]

OCA at 08:42, 18 October 2017

2017-10-18T08:42:34Z

← Older revision		Revision as of 08:42, 18 October 2017
Line 1:		Line 1:

	==Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster==		==Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster==
	<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://pdbe.org/2nvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk 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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://pdbe.org/2nvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=2nvk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	==See Also==		==See Also==
	*[[Thioredoxin Reductase\|Thioredoxin Reductase]]
	*[[User:Sarah Abdalla/Thioredoxin Reductase\|User:Sarah Abdalla/Thioredoxin Reductase]]		*[[User:Sarah Abdalla/Thioredoxin Reductase\|User:Sarah Abdalla/Thioredoxin Reductase]]
	== References ==		== References ==

OCA at 13:47, 11 September 2015

2015-09-11T13:47:30Z

← Older revision		Revision as of 13:47, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Drosophila_melanogaster Drosophila melanogaster~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVK FirstGlance]. <br>		<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 ~~Drosophila melanogaster~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk 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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://pdbe.org/2nvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/TRXR1_DROME TRXR1_DROME]] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.<ref>PMID:11158675</ref> <ref>PMID:11525742</ref> <ref>PMID:11796729</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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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 2nvk" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Drosophila melanogaster~~]]		[[Category: Drome]]
	[[Category: Thioredoxin-disulfide reductase]]		[[Category: Thioredoxin-disulfide reductase]]
	[[Category: Eckenroth, B E]]		[[Category: Eckenroth, B E]]

OCA at 13:42, 19 January 2015

2015-01-19T13:42:00Z

← Older revision		Revision as of 13:42, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVK FirstGlance]. <br>		<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVK FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk 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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Drosophila melanogaster]]		[[Category: Drosophila melanogaster]]
	[[Category: Thioredoxin-disulfide reductase]]		[[Category: Thioredoxin-disulfide reductase]]
	[[Category: Eckenroth, B E.]]		[[Category: Eckenroth, B E]]
	[[Category: Everse, S J.]]		[[Category: Everse, S J]]
	[[Category: Hondal, R J.]]		[[Category: Hondal, R J]]
	[[Category: Rould, M A.]]		[[Category: Rould, M A]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Rossmann]]		[[Category: Rossmann]]

OCA at 18:13, 30 September 2014

2014-09-30T18:13:22Z

← Older revision		Revision as of 18:13, 30 September 2014
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	~~{{STRUCTURE_2nvk~~\| ~~PDB~~=2nvk \| ~~SCENE~~= }}		==Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster==
	===~~Crystal Structure~~ of Thioredoxin ~~Reductase~~ from Drosophila melanogaster===		<StructureSection load='2nvk' size='340' side='right' caption='[[2nvk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	~~{{ABSTRACT_PUBMED_17385893}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVK FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Trxr-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2nvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nvk RCSB], [http://www.ebi.ac.uk/pdbsum/2nvk 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/nv/2nvk_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 ==
			Thioredoxin reductase (TR) from Drosophila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide disulfide oxidoreductases and catalyzes the reduction of the redox-active disulfide bond of thioredoxin. DmTR is notable for having high catalytic activity without the presence of a selenocysteine (Sec) residue (which is essential for the mammalian thioredoxin reductases). We report here the X-ray crystal structure of DmTR at 2.4 A resolution (Rwork = 19.8%, Rfree = 24.7%) in which the enzyme was truncated to remove the C-terminal tripeptide sequence Cys-Cys-Ser. We also demonstrate that tetrapeptides equivalent to the oxidized C-terminal active sites of both mouse mitochondrial TR (mTR3) and DmTR are substrates for the truncated forms of both enzymes. This truncated enzyme/peptide substrate system examines the kinetics of the ring-opening step that occurs during the enzymatic cycle of TR. The ring-opening step is 300-500-fold slower when Sec is replaced with Cys in mTR3 when using this system. Conversely, when Cys is replaced with Sec in DmTR, the rate of ring opening is only moderately increased (5-36-fold). Structures of these tetrapeptides were oriented in the active site of both enzymes using oxidized glutathione bound to GR as a template. DmTR has a more open tetrapeptide binding pocket than the mouse enzyme and accommodates the peptide Ser-Cys-Cys-Ser(ox) in a cis conformation that allows for the protonation of the leaving-group Cys by His464', which helps to explain why this TR can function without the need for Sec. In contrast, mTR3 shows a narrower pocket. One possible result of this narrower interface is that the mammalian redox-active tetrapeptide Gly-Cys-Sec-Gly may adopt a trans conformation for a better fit. This places the Sec residue farther away from the protonating histidine residue, but the lower pKa of Sec in comparison to that of Cys eliminates the need for Sec to be protonated.

	~~==About this Structure==~~		Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases.,Eckenroth BE, Rould MA, Hondal RJ, Everse SJ Biochemistry. 2007 Apr 24;46(16):4694-705. Epub 2007 Mar 27. PMID:17385893<ref>PMID:17385893</ref>
	~~[[2nvk]] is a 1 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2NVK OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==See Also==		==See Also==
	*[[Thioredoxin Reductase\|Thioredoxin Reductase]]		*[[Thioredoxin Reductase\|Thioredoxin Reductase]]
	*[[User:Sarah Abdalla/Thioredoxin Reductase\|User:Sarah Abdalla/Thioredoxin Reductase]]		*[[User:Sarah Abdalla/Thioredoxin Reductase\|User:Sarah Abdalla/Thioredoxin Reductase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:017385893<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Drosophila melanogaster]]		[[Category: Drosophila melanogaster]]
	[[Category: Thioredoxin-disulfide reductase]]		[[Category: Thioredoxin-disulfide reductase]]

OCA at 09:20, 11 March 2013

2013-03-11T09:20:17Z

← Older revision		Revision as of 09:20, 11 March 2013
Line 1:		Line 1:
	~~[[Image:2nvk.png\|left\|200px]]~~

	{{STRUCTURE_2nvk\| PDB=2nvk \| SCENE= }}		{{STRUCTURE_2nvk\| PDB=2nvk \| SCENE= }}

	===Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster===		===Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster===

	{{ABSTRACT_PUBMED_17385893}}		{{ABSTRACT_PUBMED_17385893}}

OCA at 19:21, 20 October 2012

2012-10-20T19:21:21Z

← Older revision		Revision as of 19:21, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2nvk]] is a 1 chain structure ~~of [[Thioredoxin Reductase]]~~ with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA].		[[2nvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVK OCA].

	==See Also==		==See Also==

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

2012-07-27T07:05:26Z

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

← Older revision	Revision as of 07:05, 27 July 2012
(No difference)