3dl6 - Revision history

OCA at 12:48, 30 August 2023

OCA — Wed, 30 Aug 2023 12:48:34 GMT

←Older revision		Revision as of 12:48, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='3dl6' size='340' side='right'caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>		<StructureSection load='3dl6' size='340' side='right'caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Cryho Cryho~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</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]] 3.25Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oip\|2oip]], [[3dl5\|3dl5]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [https://pdbe.org/3dl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [https://www.ebi.ac.uk/pdbsum/3dl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl6 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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [https://pdbe.org/3dl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [https://www.ebi.ac.uk/pdbsum/3dl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl6 ProSAT]</span></td></tr>
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/Q5CGA3_CRYHO Q5CGA3_CRYHO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cryho]]~~	+	[[Category: Cryptosporidium hominis]]
-	~~[[Category: Dihydrofolate reductase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Anderson~~, K S~~]]	+	[[Category: Anderson KS]]
-	[[Category: Martucci~~, W E~~]]	+	[[Category: Martucci WE]]
-	[[Category: Vargo~~, M A]]~~	+	[[Category: Vargo MA]]
-	~~[[Category: Enzyme active site mutant]]~~	+
-	~~[[Category: Enzyme-ligand complex]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 19:24, 20 October 2021

OCA — Wed, 20 Oct 2021 19:24:46 GMT

←Older revision		Revision as of 19:24, 20 October 2021
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	==Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis==		==Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis==
-	<StructureSection load='3dl6' size='340' side='right' caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>	+	<StructureSection load='3dl6' size='340' side='right'caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Cryho Cryho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryho Cryho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oip\|2oip]], [[3dl5\|3dl5]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [~~http~~://pdbe.org/3dl6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3dl6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl6 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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [https://pdbe.org/3dl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [https://www.ebi.ac.uk/pdbsum/3dl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/Q5CGA3_CRYHO Q5CGA3_CRYHO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]	+	[[https://www.uniprot.org/uniprot/Q5CGA3_CRYHO Q5CGA3_CRYHO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]	+	*[[Dihydrofolate reductase 3D structures\|Dihydrofolate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Cryho]]		[[Category: Cryho]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
		+	[[Category: Large Structures]]
	[[Category: Anderson, K S]]		[[Category: Anderson, K S]]
	[[Category: Martucci, W E]]		[[Category: Martucci, W E]]

OCA at 09:35, 14 November 2018

OCA — Wed, 14 Nov 2018 09:35:50 GMT

←Older revision		Revision as of 09:35, 14 November 2018
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dl6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dl6_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 20:52, 11 August 2016

OCA — Thu, 11 Aug 2016 20:52:34 GMT

←Older revision		Revision as of 20:52, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis==		==Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis==
	<StructureSection load='3dl6' size='340' side='right' caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>		<StructureSection load='3dl6' size='340' side='right' caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Cryptosporidium_hominis Cryptosporidium hominis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryho Cryho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 ~~Cryptosporidium hominis~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl6 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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [http://pdbe.org/3dl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl6 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q5CGA3_CRYHO Q5CGA3_CRYHO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 17:		Line 20:
	<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=3dl6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 30:
	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 3dl6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cryptosporidium hominis~~]]	+	[[Category: Cryho]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
	[[Category: Anderson, K S]]		[[Category: Anderson, K S]]

OCA at 11:25, 20 January 2015

OCA — Tue, 20 Jan 2015 11:25:18 GMT

←Older revision		Revision as of 11:25, 20 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 Cryptosporidium hominis])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 Cryptosporidium hominis])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl6 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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl6 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 36:		Line 36:
	[[Category: Cryptosporidium hominis]]		[[Category: Cryptosporidium hominis]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
-	[[Category: Anderson, K S.]]	+	[[Category: Anderson, K S]]
-	[[Category: Martucci, W E.]]	+	[[Category: Martucci, W E]]
-	[[Category: Vargo, M A.]]	+	[[Category: Vargo, M A]]
	[[Category: Enzyme active site mutant]]		[[Category: Enzyme active site mutant]]
	[[Category: Enzyme-ligand complex]]		[[Category: Enzyme-ligand complex]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 13:08, 29 September 2014

OCA — Mon, 29 Sep 2014 13:08:29 GMT

←Older revision		Revision as of 13:08, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3dl6.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis==
		+	<StructureSection load='3dl6' size='340' side='right' caption='[[3dl6]], [[Resolution\|resolution]] 3.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=DHF:DIHYDROFOLIC+ACID'>DHF</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2oip\|2oip]], [[3dl5\|3dl5]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Chro.40506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 Cryptosporidium hominis])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3dl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dl6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl6 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/dl/3dl6_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 ==
		+	The essential enzyme TS-DHFR from Cryptosporidium hominis undergoes an unusually rapid rate of catalysis at the conserved TS domain, facilitated by two nonconserved residues, Ala287 and Ser290, in the folate tail-binding region. Mutation of these two residues to their conserved counterparts drastically affects multiple steps of the TS catalytic cycle. We have determined the crystal structures of all three mutants (A287F, S290G, and A287F/S290G) in complex with active site ligands dUMP and CB3717. The structural data show two effects of the mutations: an increased distance between the ligands in the active site and increased flexibility of the folate ligand in the partially open enzyme state that precedes conformational change to the active catalytic state. The latter effect is able to be rescued by the mutants containing the A287F mutation. In addition, the conserved water network of TS is altered in each of the mutants. The structural results point to a role of the folate tail-binding residues in closely positioning ChTS ligands and restricting ligand flexibility in the partially open state to allow for a rapid transition to the active closed state and enhanced rate of catalysis. These results provide an explanation on how folate tail-binding residues at one end of the active site affect long-range interactions throughout the TS active site and validate these residues as targets for species-specific drug design.

-	~~{{STRUCTURE_3dl6\| PDB=3dl6 \| SCENE= }}~~	+	Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase.,Martucci WE, Vargo MA, Anderson KS Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:18672899<ref>PMID:18672899</ref>

-	~~===Crystal Structure~~ of the ~~A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18672899}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3dl6]] is a 5 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].~~	+

	==See Also==		==See Also==
	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]		*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
-	*[[Thymidylate synthase\|Thymidylate synthase]]	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:018672899<~~/~~ref~~><~~references group="xtra"~~/>	+	</StructureSection>
	[[Category: Cryptosporidium hominis]]		[[Category: Cryptosporidium hominis]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]

OCA at 22:27, 20 October 2012

OCA — Sat, 20 Oct 2012 22:27:33 GMT

←Older revision		Revision as of 22:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3dl6]] is a 5 chain structure ~~of [[Dihydrofolate reductase]] and [[Thymidylate synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].	+	[[3dl6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].

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

OCA: Protected "3dl6" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 16:21:40 GMT

Protected "3dl6" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:21, 27 July 2012

OCA at 16:21, 27 July 2012

OCA — Fri, 27 Jul 2012 16:21:39 GMT

←Older revision		Revision as of 16:21, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3dl6.png\|left\|200px]]		[[Image:3dl6.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3dl6", 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_3dl6\| PDB=3dl6 \| SCENE= }}		{{STRUCTURE_3dl6\| PDB=3dl6 \| SCENE= }}

	===Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis===		===Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18672899}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18672899 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18672899}}		{{ABSTRACT_PUBMED_18672899}}

	==About this Structure==		==About this Structure==
-	~~3DL6~~ is a 5 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].	+	[[3dl6]] is a 5 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]] with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].
		+
		+	==See Also==
		+	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
		+	*[[Thymidylate synthase\|Thymidylate synthase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18672899~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018672899</ref><references group="xtra"/>
	[[Category: Cryptosporidium hominis]]		[[Category: Cryptosporidium hominis]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
Line 32:		Line 24:
	[[Category: Enzyme-ligand complex]]		[[Category: Enzyme-ligand complex]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:53:37 2009''

OCA at 07:53, 18 February 2009

OCA — Wed, 18 Feb 2009 07:53:39 GMT

←Older revision		Revision as of 07:53, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	3DL6 is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].	+	3DL6 is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].

	==Reference==		==Reference==
-	Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase., Martucci WE, Vargo MA, Anderson KS, Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18672899 18672899]~~	+	<ref group="xtra">PMID:18672899</ref><references group="xtra"/>
	[[Category: Cryptosporidium hominis]]		[[Category: Cryptosporidium hominis]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
-	[[Category: Single protein]]
	[[Category: Anderson, K S.]]		[[Category: Anderson, K S.]]
	[[Category: Martucci, W E.]]		[[Category: Martucci, W E.]]
Line 34:		Line 33:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Sep 3 10~~:34:~~02 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:53:37 2009''