2orw: Difference between revisions
New page: left|200px<br /><applet load="2orw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2orw, resolution 1.500Å" /> '''Thermotoga maritima... |
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[[Image:2orw.jpg|left|200px]]<br /><applet load="2orw" size=" | [[Image:2orw.jpg|left|200px]]<br /><applet load="2orw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2orw, resolution 1.500Å" /> | caption="2orw, resolution 1.500Å" /> | ||
'''Thermotoga maritima thymidine kinase 1 like enzyme in complex with TP4A'''<br /> | '''Thermotoga maritima thymidine kinase 1 like enzyme in complex with TP4A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2ORW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ZN, MG and 4TA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidine_kinase Thymidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.21 2.7.1.21] Full crystallographic information is available from [http:// | 2ORW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=4TA:'>4TA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidine_kinase Thymidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.21 2.7.1.21] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tp4a]] | [[Category: tp4a]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:40 2008'' | ||
Revision as of 16:09, 23 January 2008
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Thermotoga maritima thymidine kinase 1 like enzyme in complex with TP4A
OverviewOverview
Human thymidine kinase 1 (hTK1) and structurally related TKs from other, organisms catalyze the initial phosphorylation step in the thymidine, salvage pathway. Though ATP is known to be the preferred phosphoryl donor, for TK1-like enzymes, its exact binding mode and effect on the oligomeric, state has not been analyzed. Here we report the structures of hTK1 and of, the Thermotoga maritima thymidine kinase (TmTK) in complex with the, bisubstrate inhibitor TP4A. The TmTK-TP4A structure reveals that the, adenosine moiety of ATP binds at the subunit interface of the, homotetrameric enzyme and that the majority of the ATP-enzyme interactions, occur between the phosphate groups and the P-loop. In the hTK1 structure, the adenosine group of TP4A exhibited no electron density. This difference, between hTK1 and TmTK is rationalized by a difference in the conformation, of their quaternary structure. A more open conformation, as seen in the, TmTK-TP4A complex structure, is required to provide space for the, adenosine moiety. Our analysis supports the formation of an analogous open, conformation in hTK1 upon ATP binding.
About this StructureAbout this Structure
2ORW is a Single protein structure of sequence from Thermotoga maritima with , and as ligands. Active as Thymidine kinase, with EC number 2.7.1.21 Full crystallographic information is available from OCA.
ReferenceReference
Binding of ATP to TK1-like Enzymes Is Associated with a Conformational Change in the Quaternary Structure., Segura-Pena D, Lutz S, Monnerjahn C, Konrad M, Lavie A, J Mol Biol. 2007 May 25;369(1):129-41. Epub 2007 Mar 15. PMID:17407781
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