4gtd - Revision history

OCA at 15:55, 14 March 2024

2024-03-14T15:55:56Z

←Older revision		Revision as of 15:55, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GTD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GTD 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=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]] 1.76Å</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=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [https://pdbe.org/4gtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [https://www.ebi.ac.uk/pdbsum/4gtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtd 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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [https://pdbe.org/4gtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [https://www.ebi.ac.uk/pdbsum/4gtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.		[https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The DNA nucleotide thymidylate is synthesized by the enzyme thymidylate synthase, which catalyzes the reductive methylation of deoxyuridylate using the cofactor methylene-tetrahydrofolate (CH(2)H(4)folate). Most organisms, including humans, rely on the thyA- or TYMS-encoded classic thymidylate synthase, whereas, certain microorganisms, including all Rickettsia and other pathogens, use an alternative thyX-encoded flavin-dependent thymidylate synthase (FDTS). Although several crystal structures of FDTSs have been reported, the absence of a structure with folates limits understanding of the molecular mechanism and the scope of drug design for these enzymes. Here we present X-ray crystal structures of FDTS with several folate derivatives, which together with mutagenesis, kinetic analysis, and computer modeling shed light on the cofactor binding and function. The unique structural data will likely facilitate further elucidation of FDTSs' mechanism and the design of structure-based inhibitors as potential leads to new antimicrobial drugs.
-
-	Folate binding site of flavin-dependent thymidylate synthase.,Koehn EM, Perissinotti LL, Moghram S, Prabhakar A, Lesley SA, Mathews II, Kohen A Proc Natl Acad Sci U S A. 2012 Sep 25;109(39):15722-7. Epub 2012 Sep 10. PMID:23019356<ref>PMID:23019356</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gtd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thymidylate synthase 3D structures\|Thymidylate synthase 3D structures]]		*[[Thymidylate synthase 3D structures\|Thymidylate synthase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:16, 26 October 2022

2022-10-26T07:16:56Z

←Older revision		Revision as of 07:16, 26 October 2022
Line 1:		Line 1:

	==T. Maritima FDTS (E144R mutant) with FAD and dUMP==		==T. Maritima FDTS (E144R mutant) with FAD and dUMP==
-	<StructureSection load='4gtd' size='340' side='right' caption='[[4gtd]], [[Resolution\|resolution]] 1.76Å' scene=''>	+	<StructureSection load='4gtd' size='340' side='right'caption='[[4gtd]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Thema Thema~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GTD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GTD 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=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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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">thyX, thy1, TM_0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [https://pdbe.org/4gtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [https://www.ebi.ac.uk/pdbsum/4gtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtd ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] </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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [~~http~~://pdbe.org/4gtd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gtd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtd ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA]] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.	+	[https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Thymidylate synthase\|Thymidylate synthase]]	+	*[[Thymidylate synthase 3D structures\|Thymidylate synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Thema~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Kohen, A~~]]	+	[[Category: Thermotoga maritima MSB8]]
-	[[Category: ~~Lesley, S~~ A]]	+	[[Category: Kohen A]]
-	[[Category: ~~Mathews, I I~~]]	+	[[Category: Lesley SA]]
-	[[Category: ~~Prabhakar, A~~]]	+	[[Category: Mathews II]]
-	[[Category: ~~E144r mutant]]~~	+	[[Category: Prabhakar A]]
-	~~[[Category: Flavin-dependent thymidylate synthase]]~~	+
-	~~[[Category: Tm0449]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 12:07, 4 August 2016

2016-08-04T12:07:06Z

←Older revision		Revision as of 12:07, 4 August 2016
Line 1:		Line 1:
		+
	==T. Maritima FDTS (E144R mutant) with FAD and dUMP==		==T. Maritima FDTS (E144R mutant) with FAD and dUMP==
	<StructureSection load='4gtd' size='340' side='right' caption='[[4gtd]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='4gtd' size='340' side='right' caption='[[4gtd]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermotoga_maritima_msb8 Thermotoga maritima msb8~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GTD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GTD 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=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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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">thyX, thy1, TM_0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 ~~Thermotoga maritima MSB8~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">thyX, thy1, TM_0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] </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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [http://www.ebi.ac.uk/pdbsum/4gtd 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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [http://pdbe.org/4gtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [http://www.ebi.ac.uk/pdbsum/4gtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4gtd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thymidylate synthase\|Thymidylate synthase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Thermotoga maritima msb8~~]]	+	[[Category: Thema]]
	[[Category: Kohen, A]]		[[Category: Kohen, A]]
	[[Category: Lesley, S A]]		[[Category: Lesley, S A]]

OCA at 09:09, 25 December 2014

2014-12-25T09:09:57Z

←Older revision		Revision as of 09:09, 25 December 2014
Line 8:		Line 8:
	<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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [http://www.ebi.ac.uk/pdbsum/4gtd 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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [http://www.ebi.ac.uk/pdbsum/4gtd PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA]] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:08, 10 December 2014

2014-12-10T09:08:23Z

←Older revision		Revision as of 09:08, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gtd.~~jpg~~\|~~left~~\|~~200px~~]]	+	==T. Maritima FDTS (E144R mutant) with FAD and dUMP==
		+	<StructureSection load='4gtd' size='340' side='right' caption='[[4gtd]], [[Resolution\|resolution]] 1.76Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gtd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GTD 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=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">thyX, thy1, TM_0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] </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=4gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gtd RCSB], [http://www.ebi.ac.uk/pdbsum/4gtd PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The DNA nucleotide thymidylate is synthesized by the enzyme thymidylate synthase, which catalyzes the reductive methylation of deoxyuridylate using the cofactor methylene-tetrahydrofolate (CH(2)H(4)folate). Most organisms, including humans, rely on the thyA- or TYMS-encoded classic thymidylate synthase, whereas, certain microorganisms, including all Rickettsia and other pathogens, use an alternative thyX-encoded flavin-dependent thymidylate synthase (FDTS). Although several crystal structures of FDTSs have been reported, the absence of a structure with folates limits understanding of the molecular mechanism and the scope of drug design for these enzymes. Here we present X-ray crystal structures of FDTS with several folate derivatives, which together with mutagenesis, kinetic analysis, and computer modeling shed light on the cofactor binding and function. The unique structural data will likely facilitate further elucidation of FDTSs' mechanism and the design of structure-based inhibitors as potential leads to new antimicrobial drugs.

-	~~{{STRUCTURE_4gtd\| PDB=4gtd \| SCENE= }}~~	+	Folate binding site of flavin-dependent thymidylate synthase.,Koehn EM, Perissinotti LL, Moghram S, Prabhakar A, Lesley SA, Mathews II, Kohen A Proc Natl Acad Sci U S A. 2012 Sep 25;109(39):15722-7. Epub 2012 Sep 10. PMID:23019356<ref>PMID:23019356</ref>

-	~~===T~~. ~~Maritima FDTS (E144R mutant) with FAD and dUMP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23019356}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4gtd]] is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA].~~	+	</StructureSection>
	[[Category: Thermotoga maritima msb8]]		[[Category: Thermotoga maritima msb8]]
-	[[Category: Kohen, A.]]	+	[[Category: Kohen, A]]
-	[[Category: Lesley, S A.]]	+	[[Category: Lesley, S A]]
-	[[Category: Mathews, I I.]]	+	[[Category: Mathews, I I]]
-	[[Category: Prabhakar, A.]]	+	[[Category: Prabhakar, A]]
	[[Category: E144r mutant]]		[[Category: E144r mutant]]
	[[Category: Flavin-dependent thymidylate synthase]]		[[Category: Flavin-dependent thymidylate synthase]]
	[[Category: Tm0449]]		[[Category: Tm0449]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:55, 17 October 2012

2012-10-17T06:55:05Z

←Older revision		Revision as of 06:55, 17 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gtd.jpg\|left\|200px]]

-	~~The entry~~ 4gtd ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gtd\| PDB=4gtd \| SCENE= }}

-	~~Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A~~.	+	===T. Maritima FDTS (E144R mutant) with FAD and dUMP===

-	~~Description~~: T. ~~Maritima FDTS (E144R~~ mutant~~) with FAD and dUMP~~	+	{{ABSTRACT_PUBMED_23019356}}
		+
		+	==About this Structure==
		+	[[4gtd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTD OCA].
		+	[[Category: Thermotoga maritima msb8]]
		+	[[Category: Kohen, A.]]
		+	[[Category: Lesley, S A.]]
		+	[[Category: Mathews, I I.]]
		+	[[Category: Prabhakar, A.]]
		+	[[Category: E144r mutant]]
		+	[[Category: Flavin-dependent thymidylate synthase]]
		+	[[Category: Tm0449]]
		+	[[Category: Transferase]]

OCA at 06:53, 10 October 2012

2012-10-10T06:53:45Z

←Older revision		Revision as of 06:53, 10 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gtd is ON HOLD	+	The entry 4gtd is ON HOLD until Paper Publication

	Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A.		Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A.

	Description: T. Maritima FDTS (E144R mutant) with FAD and dUMP		Description: T. Maritima FDTS (E144R mutant) with FAD and dUMP

OCA: Protected "4gtd" [edit=sysop:move=sysop]

2012-09-05T04:58:39Z

Protected "4gtd" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:58, 5 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gtd is ON HOLD Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A. Description: T. Maritima FDTS (E144R mutant) with FAD and dUMP

2012-09-05T04:58:38Z

New page: '''Unreleased structure''' The entry 4gtd is ON HOLD Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A. Description: T. Maritima FDTS (E144R mutant) with FAD and dUMP

New page

'''Unreleased structure'''

The entry 4gtd is ON HOLD

Authors: Mathews, I.I., Lesley, S.A., Kohen, A., Prabhakar, A.

Description: T. Maritima FDTS (E144R mutant) with FAD and dUMP