1p73 | pdb_00001p73

Crystal structure of EHV4-TK complexed with TP4A

spinqualitylabelsall models 1p73, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1p73 is a 4 chain structure with sequence from Equid herpesvirus 4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 4TA, SO4 Related: 1p72, 1p6x, 1p75, 1p7c Gene: TK (Equid herpesvirus 4) Activity: Thymidine kinase, with EC number 2.7.1.21 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thymidine kinase

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