1p72

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(New page: 200px<br /><applet load="1p72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p72, resolution 2.10&Aring;" /> '''Crystal structure of...)
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caption="1p72, resolution 2.10&Aring;" />
'''Crystal structure of EHV4-TK complexed with Thy and ADP'''<br />
'''Crystal structure of EHV4-TK complexed with Thy and ADP'''<br />
==Overview==
==Overview==
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Crystal structures of equine herpesvirus type-4 thymidine kinase (EHV4-TK), in complex with (i). thymidine and ADP, (ii). thymidine and SO(4) and the, bisubstrate analogs, (iii). TP(4)A, and (iv). TP(5)A have been solved., Additionally, the structure of herpes simplex virus type-1 thymidine, kinase (HSV1-TK) in complex with TP(5)A has been determined. These are the, first structures of nucleoside kinases revealing conformational, transitions upon binding of bisubstrate analogs. The structural basis for, the dual thymidine and thymidylate kinase activity of these TKs is, elucidated. While the active sites of HSV1-TK and EHV4-TK resemble one, another, notable differences are observed in the Lid regions and in the, way the enzymes bind the base of the phosphoryl-acceptor. The latter, difference could partly explain the higher activity of EHV4-TK toward the, prodrug ganciclovir.
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Crystal structures of equine herpesvirus type-4 thymidine kinase (EHV4-TK) in complex with (i). thymidine and ADP, (ii). thymidine and SO(4) and the bisubstrate analogs, (iii). TP(4)A, and (iv). TP(5)A have been solved. Additionally, the structure of herpes simplex virus type-1 thymidine kinase (HSV1-TK) in complex with TP(5)A has been determined. These are the first structures of nucleoside kinases revealing conformational transitions upon binding of bisubstrate analogs. The structural basis for the dual thymidine and thymidylate kinase activity of these TKs is elucidated. While the active sites of HSV1-TK and EHV4-TK resemble one another, notable differences are observed in the Lid regions and in the way the enzymes bind the base of the phosphoryl-acceptor. The latter difference could partly explain the higher activity of EHV4-TK toward the prodrug ganciclovir.
==About this Structure==
==About this Structure==
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1P72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equid_herpesvirus_4 Equid herpesvirus 4] with SO4, ADP and THM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P72 OCA].
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1P72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equid_herpesvirus_4 Equid herpesvirus 4] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=THM:'>THM</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=1P72 OCA].
==Reference==
==Reference==
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[[Category: p-loop]]
[[Category: p-loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:32:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:48 2008''

Revision as of 12:25, 21 February 2008

Image:1p72.jpg

1p72, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of EHV4-TK complexed with Thy and ADP

Overview

Crystal structures of equine herpesvirus type-4 thymidine kinase (EHV4-TK) in complex with (i). thymidine and ADP, (ii). thymidine and SO(4) and the bisubstrate analogs, (iii). TP(4)A, and (iv). TP(5)A have been solved. Additionally, the structure of herpes simplex virus type-1 thymidine kinase (HSV1-TK) in complex with TP(5)A has been determined. These are the first structures of nucleoside kinases revealing conformational transitions upon binding of bisubstrate analogs. The structural basis for the dual thymidine and thymidylate kinase activity of these TKs is elucidated. While the active sites of HSV1-TK and EHV4-TK resemble one another, notable differences are observed in the Lid regions and in the way the enzymes bind the base of the phosphoryl-acceptor. The latter difference could partly explain the higher activity of EHV4-TK toward the prodrug ganciclovir.

About this Structure

1P72 is a Single protein structure of sequence from Equid herpesvirus 4 with , and as ligands. Active as Thymidine kinase, with EC number 2.7.1.21 Full crystallographic information is available from OCA.

Reference

Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases., Gardberg A, Shuvalova L, Monnerjahn C, Konrad M, Lavie A, Structure. 2003 Oct;11(10):1265-77. PMID:14527394

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