1P72

Crystal structure of EHV4-TK complexed with Thy and ADP

1P72 の概要

• エントリーDOI: 10.2210/pdb1p72/pdb
• 関連するPDBエントリー: 1P6X 1P73 1P75 1P7C
• 分子名称: Thymidine kinase, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: p-loop, lid, transferase
• 由来する生物種: Equid herpesvirus 4 (Equine herpesvirus 4)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76230.03

構造登録者

Gardberg, A.,Shuvalova, L.,Monnerjahn, C.,Konrad, M.,Lavie, A. (登録日: 2003-04-30, 公開日: 2003-11-04, 最終更新日: 2023-08-16)

主引用文献

Gardberg, A.,Shuvalova, L.,Monnerjahn, C.,Konrad, M.,Lavie, A.
Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.
Structure, 11:1265-1277, 2003

PubMed Abstract: 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.

PubMed: 14527394
DOI: 10.1016/j.str.2003.09.003

実験手法

X-RAY DIFFRACTION (2.1 Å)