2tpr - Revision history

OCA at 12:29, 23 March 2022

2022-03-23T12:29:08Z

←Older revision		Revision as of 12:29, 23 March 2022
Line 3:		Line 3:
	<StructureSection load='2tpr' size='340' side='right'caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2tpr' size='340' side='right'caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2TPR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TPR 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></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></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [~~http~~://pdbe.org/2tpr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2tpr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpr 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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [https://pdbe.org/2tpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [https://www.ebi.ac.uk/pdbsum/2tpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TYTR_CRIFA TYTR_CRIFA]] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.	+	[[https://www.uniprot.org/uniprot/TYTR_CRIFA TYTR_CRIFA]] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:08, 17 June 2020

2020-06-17T11:08:55Z

←Older revision		Revision as of 11:08, 17 June 2020
Line 1:		Line 1:

	==X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION==		==X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION==
-	<StructureSection load='2tpr' size='340' side='right' caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='2tpr' size='340' side='right'caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2TPR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2TPR 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></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></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://pdbe.org/2tpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpr ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://pdbe.org/2tpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Crifa]]		[[Category: Crifa]]
		+	[[Category: Large Structures]]
	[[Category: Trypanothione-disulfide reductase]]		[[Category: Trypanothione-disulfide reductase]]
	[[Category: Kong, X P]]		[[Category: Kong, X P]]

OCA at 08:55, 12 September 2018

2018-09-12T08:55:39Z

←Older revision		Revision as of 08:55, 12 September 2018
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/2tpr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/2tpr_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 02:20, 5 August 2016

2016-08-05T02:20:55Z

←Older revision		Revision as of 02:20, 5 August 2016
Line 1:		Line 1:
		+
	==X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION==		==X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION==
	<StructureSection load='2tpr' size='340' side='right' caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2tpr' size='340' side='right' caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Crithidia_fasciculata Crithidia fasciculata~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TPR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TPR 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></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></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr 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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://pdbe.org/2tpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<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=2tpr 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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	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 2tpr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Crithidia fasciculata~~]]	+	[[Category: Crifa]]
	[[Category: Trypanothione-disulfide reductase]]		[[Category: Trypanothione-disulfide reductase]]
	[[Category: Kong, X P]]		[[Category: Kong, X P]]

OCA at 15:03, 25 December 2014

2014-12-25T15:03:38Z

←Older revision		Revision as of 15:03, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TPR FirstGlance]. <br>		<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TPR 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><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></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr 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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TYTR_CRIFA TYTR_CRIFA]] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: Crithidia fasciculata]]		[[Category: Crithidia fasciculata]]
	[[Category: Trypanothione-disulfide reductase]]		[[Category: Trypanothione-disulfide reductase]]
-	[[Category: Kong, X P.]]	+	[[Category: Kong, X P]]
-	[[Category: Krishna, T S.R.]]	+	[[Category: Krishna, T S.R]]
-	[[Category: Kuriyan, J.]]	+	[[Category: Kuriyan, J]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 02:18, 1 October 2014

2014-10-01T02:18:26Z

←Older revision		Revision as of 02:18, 1 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2tpr\| PDB=2tpr \| SCENE= }}~~	+	==X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION==
-	===X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION===	+	<StructureSection load='2tpr' size='340' side='right' caption='[[2tpr]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_1924336}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2tpr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TPR 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><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </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=2tpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2tpr RCSB], [http://www.ebi.ac.uk/pdbsum/2tpr 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/tp/2tpr_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 ==
		+	Trypanosomes and related protozoan parasites lack glutathione reductase and possess instead a closely related enzyme that serves as the reductant of a bis(glutathione)-spermidine conjugate, trypanothione. The human and parasite enzymes have mutually exclusive substrate specificities, providing a route for the design of therapeutic agents by specific inhibition of the parasite enzyme. We report here the three-dimensional structure of trypanothione reductase from Crithidia fasciculata and show that it closely resembles the structure of human glutathione reductase. In particular, the core structure surrounding the catalytic machinery is almost identical in the two enzymes. However, significant differences are found at the substrate binding sites. A cluster of basic residues in glutathione reductase is replaced by neutral, hydrophobic, or acidic residues in trypanothione reductase, consistent with the nature of the spermidine linkage and the change in overall charge of the substrate from -2 to +1, respectively. The binding site is more open in trypanothione reductase due to rotations of about 4 degrees in the domains that form the site, with relative shifts of as much as 2-3 A in residue positions. These results provide a detailed view of the residues that can interact with potential inhibitors and complement previous modeling and mutagenesis studies on the two enzymes.

-	~~==About this Structure==~~	+	X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution.,Kuriyan J, Kong XP, Krishna TS, Sweet RM, Murgolo NJ, Field H, Cerami A, Henderson GB Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8764-8. PMID:1924336<ref>PMID:1924336</ref>
-	~~[[2tpr]] is a 2 chain~~ structure ~~with sequence~~ from ~~[http://en.wikipedia.org/wiki/Crithidia_fasciculata~~ Crithidia fasciculata]. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2TPR OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Trypanothione reductase\|Trypanothione reductase]]		*[[Trypanothione reductase\|Trypanothione reductase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:001924336<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Crithidia fasciculata]]		[[Category: Crithidia fasciculata]]
	[[Category: Trypanothione-disulfide reductase]]		[[Category: Trypanothione-disulfide reductase]]

OCA at 11:12, 11 March 2013

2013-03-11T11:12:29Z

←Older revision		Revision as of 11:12, 11 March 2013
Line 1:		Line 1:
-	[[Image:2tpr.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_2tpr", 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.
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	{{STRUCTURE_2tpr\| PDB=2tpr \| SCENE= }}		{{STRUCTURE_2tpr\| PDB=2tpr \| SCENE= }}
-
	===X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION===		===X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS RESOLUTION===
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-	The line below this paragraph, {{ABSTRACT_PUBMED_1924336}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_1924336}}		{{ABSTRACT_PUBMED_1924336}}

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

2012-06-02T09:45:44Z

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

←Older revision

Revision as of 09:45, 2 June 2012