2orv

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[[Image:2orv.gif|left|200px]]<br /><applet load="2orv" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2orv.gif|left|200px]]
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caption="2orv, resolution 2.300&Aring;" />
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'''human Thymidine Kinase 1 in complex with TP4A'''<br />
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{{Structure
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|PDB= 2orv |SIZE=350|CAPTION= <scene name='initialview01'>2orv</scene>, resolution 2.300&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=4TA:P1-(5'-ADENOSYL)P4-(5'-(2'-DEOXY-THYMIDYL))TETRAPHOSPHATE'>4TA</scene>
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|ACTIVITY= [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]
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|GENE= TK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''human Thymidine Kinase 1 in complex with TP4A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ORV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</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=2ORV OCA].
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2ORV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORV OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17407781 17407781]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17407781 17407781]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tp4a (p1-(5'-adenosyl)p4-(5'-(2'deoxythymidil))tetraphosphate]]
[[Category: tp4a (p1-(5'-adenosyl)p4-(5'-(2'deoxythymidil))tetraphosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:03:42 2008''

Revision as of 16:03, 20 March 2008


PDB ID 2orv

Drag the structure with the mouse to rotate
, resolution 2.300Å
Ligands: and
Gene: TK1 (Homo sapiens)
Activity: Thymidine kinase, with EC number 2.7.1.21
Coordinates: save as pdb, mmCIF, xml



human Thymidine Kinase 1 in complex with TP4A


Overview

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 Structure

2ORV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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