4s2e - Revision history

OCA at 18:01, 20 September 2023

OCA — Wed, 20 Sep 2023 18:01:54 GMT

←Older revision		Revision as of 18:01, 20 September 2023
Line 1:		Line 1:

	==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==		==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==
-	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]]' scene=''>	+	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2E FirstGlance]. <br>
-	</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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [https://pdbe.org/4s2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [https://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></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]] 2.35Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [https://pdbe.org/4s2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [https://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Thymidylate kinase (TMK) is a key enzyme which plays an important role in DNA synthesis. It belongs to the family of nucleoside monophosphate kinases, several of which undergo structure-encoded conformational changes to perform their function. However, the absence of three-dimensional structures for all the different reaction intermediates of a single TMK homolog hinders a clear understanding of its functional mechanism. We herein report the different conformational states along the reaction coordinate of a hyperthermophilic TMK from Aquifex aeolicus, determined via X-ray diffraction and further validated through normal-mode studies. The analyses implicate an arginine residue in the Lid region in catalysis, which was confirmed through site-directed mutagenesis and subsequent enzyme assays on the wild-type protein and mutants. Furthermore, the enzyme was found to exhibit broad specificity toward phosphate group acceptor nucleotides. Our comprehensive analyses of the conformational landscape of TMK, together with associated biochemical experiments, provide insights into the mechanistic details of TMK-driven catalysis, for example, the order of substrate binding and the reaction mechanism for phosphate transfer. Such a study has utility in the design of potent inhibitors for these enzymes. DATABASE: Structural data are available in the PDB under the accession numbers 2PBR, 4S2E, 5H5B, 5XAI, 4S35, 5XB2, 5H56, 5XB3, 5H5K, 5XB5, and 5XBH.
		+
		+	Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.,Biswas A, Shukla A, Chaudhary SK, Santhosh R, Jeyakanthan J, Sekar K FEBS J. 2017 Aug;284(15):2527-2544. doi: 10.1111/febs.14140. Epub 2017 Jul 13. PMID:28627020<ref>PMID:28627020</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4s2e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]		*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aquifex aeolicus VF5]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Biswas A]]		[[Category: Biswas A]]
	[[Category: Jeyakanthan J]]		[[Category: Jeyakanthan J]]
	[[Category: Sekar K]]		[[Category: Sekar K]]

OCA at 11:00, 31 August 2022

OCA — Wed, 31 Aug 2022 11:00:27 GMT

←Older revision		Revision as of 11:00, 31 August 2022
Line 1:		Line 1:

	==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==		==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==
-	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]]~~, [[Resolution\|resolution]] 2.35Å~~' scene=''>	+	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[4s2e]] is a 2 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2E FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2E FirstGlance]. <br>
-	</td></tr>~~<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>~~	+	</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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [https://pdbe.org/4s2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [https://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pbr\|2pbr]]</div></td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [https://pdbe.org/4s2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [https://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Thymidylate kinase (TMK) is a key enzyme which plays an important role in DNA synthesis. It belongs to the family of nucleoside monophosphate kinases, several of which undergo structure-encoded conformational changes to perform their function. However, the absence of three-dimensional structures for all the different reaction intermediates of a single TMK homolog hinders a clear understanding of its functional mechanism. We herein report the different conformational states along the reaction coordinate of a hyperthermophilic TMK from Aquifex aeolicus, determined via X-ray diffraction and further validated through normal-mode studies. The analyses implicate an arginine residue in the Lid region in catalysis, which was confirmed through site-directed mutagenesis and subsequent enzyme assays on the wild-type protein and mutants. Furthermore, the enzyme was found to exhibit broad specificity toward phosphate group acceptor nucleotides. Our comprehensive analyses of the conformational landscape of TMK, together with associated biochemical experiments, provide insights into the mechanistic details of TMK-driven catalysis, for example, the order of substrate binding and the reaction mechanism for phosphate transfer. Such a study has utility in the design of potent inhibitors for these enzymes. DATABASE: Structural data are available in the PDB under the accession numbers 2PBR, 4S2E, 5H5B, 5XAI, 4S35, 5XB2, 5H56, 5XB3, 5H5K, 5XB5, and 5XBH.
-
-	Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.,Biswas A, Shukla A, Chaudhary SK, Santhosh R, Jeyakanthan J, Sekar K FEBS J. 2017 Aug;284(15):2527-2544. doi: 10.1111/febs.14140. Epub 2017 Jul 13. PMID:28627020<ref>PMID:28627020</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4s2e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]		*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: DTMP kinase]]~~	+	[[Category: Biswas A]]
-	[[Category: Biswas, A]]	+	[[Category: Jeyakanthan J]]
-	[[Category: Jeyakanthan, J]]	+	[[Category: Sekar K]]
-	[[Category: Sekar, K]]	+
-	~~[[Category: Atp binding]]~~	+
-	~~[[Category: Tmp binding]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:09, 25 August 2022

OCA — Thu, 25 Aug 2022 05:09:15 GMT

←Older revision		Revision as of 05:09, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4S2E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2pbr\|2pbr]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pbr\|2pbr]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [~~http~~://pdbe.org/4s2e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e 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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [https://pdbe.org/4s2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [https://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).	+	[[https://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Thymidylate kinase (TMK) is a key enzyme which plays an important role in DNA synthesis. It belongs to the family of nucleoside monophosphate kinases, several of which undergo structure-encoded conformational changes to perform their function. However, the absence of three-dimensional structures for all the different reaction intermediates of a single TMK homolog hinders a clear understanding of its functional mechanism. We herein report the different conformational states along the reaction coordinate of a hyperthermophilic TMK from Aquifex aeolicus, determined via X-ray diffraction and further validated through normal-mode studies. The analyses implicate an arginine residue in the Lid region in catalysis, which was confirmed through site-directed mutagenesis and subsequent enzyme assays on the wild-type protein and mutants. Furthermore, the enzyme was found to exhibit broad specificity toward phosphate group acceptor nucleotides. Our comprehensive analyses of the conformational landscape of TMK, together with associated biochemical experiments, provide insights into the mechanistic details of TMK-driven catalysis, for example, the order of substrate binding and the reaction mechanism for phosphate transfer. Such a study has utility in the design of potent inhibitors for these enzymes. DATABASE: Structural data are available in the PDB under the accession numbers 2PBR, 4S2E, 5H5B, 5XAI, 4S35, 5XB2, 5H56, 5XB3, 5H5K, 5XB5, and 5XBH.
		+
		+	Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.,Biswas A, Shukla A, Chaudhary SK, Santhosh R, Jeyakanthan J, Sekar K FEBS J. 2017 Aug;284(15):2527-2544. doi: 10.1111/febs.14140. Epub 2017 Jul 13. PMID:28627020<ref>PMID:28627020</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4s2e" style="background-color:#fffaf0;"></div>

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

OCA at 18:02, 14 August 2019

OCA — Wed, 14 Aug 2019 18:02:22 GMT

←Older revision		Revision as of 18:02, 14 August 2019
Line 1:		Line 1:

	==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==		==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==
-	<StructureSection load='4s2e' size='340' side='right' caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>	+	<StructureSection load='4s2e' size='340' side='right'caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2E FirstGlance]. <br>
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).		[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
		+
		+	==See Also==
		+	*[[Thymidylate kinase\|Thymidylate kinase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Biswas, A]]		[[Category: Biswas, A]]

OCA at 12:37, 6 November 2017

OCA — Mon, 06 Nov 2017 12:37:25 GMT

←Older revision		Revision as of 12:37, 6 November 2017
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).		[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
-
-	==See Also==
-	*[[Thymidylate kinase\|Thymidylate kinase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:15, 3 August 2017

OCA — Thu, 03 Aug 2017 09:15:10 GMT

←Older revision		Revision as of 09:15, 3 August 2017
Line 1:		Line 1:
		+
	==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==		==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==
	<StructureSection load='4s2e' size='340' side='right' caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='4s2e' size='340' side='right' caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2pbr\|2pbr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2pbr\|2pbr]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [http://pdbe.org/4s2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [http://www.ebi.ac.uk/pdbsum/4s2e 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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [http://pdbe.org/4s2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [http://www.ebi.ac.uk/pdbsum/4s2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).		[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
		+
		+	==See Also==
		+	*[[Thymidylate kinase\|Thymidylate kinase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:10, 20 January 2016

OCA — Wed, 20 Jan 2016 17:10:09 GMT

←Older revision		Revision as of 17:10, 20 January 2016
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5==
-		+	<StructureSection load='4s2e' size='340' side='right' caption='[[4s2e]], [[Resolution\|resolution]] 2.35Å' scene=''>
-	~~The entry~~ 4s2e is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4s2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2E FirstGlance]. <br>
-	~~Authors~~: ~~Biswas~~, A., ~~Jeyakanthan~~, J., ~~Sekar~~, K.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2pbr\|2pbr]]</td></tr>
-	~~Description~~: ~~Phosphate ion bound Crystal structure~~ of ~~thymidylate kinase~~ (~~aq_969~~) ~~from Aquifex Aeolicus VF5~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=4s2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2e OCA], [http://pdbe.org/4s2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2e RCSB], [http://www.ebi.ac.uk/pdbsum/4s2e PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KTHY_AQUAE KTHY_AQUAE]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: DTMP kinase]]
	[[Category: Biswas, A]]		[[Category: Biswas, A]]
	[[Category: Jeyakanthan, J]]		[[Category: Jeyakanthan, J]]
	[[Category: Sekar, K]]		[[Category: Sekar, K]]
		+	[[Category: Atp binding]]
		+	[[Category: Tmp binding]]
		+	[[Category: Transferase]]

OCA at 08:19, 11 March 2015

OCA — Wed, 11 Mar 2015 08:19:30 GMT

←Older revision		Revision as of 08:19, 11 March 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4s2e is ON HOLD	+	The entry 4s2e is ON HOLD until Paper Publication

	Authors: Biswas, A., Jeyakanthan, J., Sekar, K.		Authors: Biswas, A., Jeyakanthan, J., Sekar, K.

OCA at 12:52, 7 February 2015

OCA — Sat, 07 Feb 2015 12:52:49 GMT

←Older revision		Revision as of 12:52, 7 February 2015
Line 3:		Line 3:
	The entry 4s2e is ON HOLD		The entry 4s2e is ON HOLD

-	Authors: Biswas, A, Jeyakanthan, J, Sekar, K	+	Authors: Biswas, A., Jeyakanthan, J., Sekar, K.

	Description: Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5		Description: Phosphate ion bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Biswas, A, Jeyakanthan, J, Sekar, K]]	+	[[Category: Biswas, A]]
		+	[[Category: Jeyakanthan, J]]
		+	[[Category: Sekar, K]]

OCA: Protected "4s2e" [edit=sysop:move=sysop]

OCA — Wed, 28 Jan 2015 13:37:37 GMT

Protected "4s2e" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:37, 28 January 2015