1p72
From Proteopedia
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | TK (Equid herpesvirus 4) | ||||||
| Activity: | Thymidine kinase, with EC number 2.7.1.21 | ||||||
| Related: | 1P6X, 1P73, 1P75, 1P7C
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:55:48 2008
