The three‐dimensional structure of thymidine kinase from Herpes simplex virus type 1

FEBS Letters

Aubry, André²  Folkers, Gerd³  Schulz, Georg E.¹  Bohner, Thomas³  Wild, Klemens¹ 

[1] Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstr. 21, Freiburg im Breisgau, Germany;LCM3B, Univesité Henri Poincaré, Nancy I, Vandoeuvre Cedex, France;Department Pharmazie, Eidgenössische Technische Hochschule, Zürich, Switzerland

关键词: Thymidine kinase;    Herpes simplex virus;    X-Ray analysis;    Phosphoryl transfer;    Chain fold;    DTT;    dithiothreitol;    HSV1;    Herpes simplex virus type 1;    PEG;    polyethylene-glycol;    TK;    thymidine kinase;   

DOI  :  10.1016/0014-5793(95)00680-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant thymidine kinase from Herpes simplex virus type 1 (ATP:thymidine 5′-phosphotransferase; EC 2.7.1.21), an enzyme of therapeutic importance, was purified and crystallized in an N-terminally truncated but still fully active form. The three-dimensional structure was solved by X-ray diffraction analysis at 3.0 Å resolution using isomorphous replacement. The chain fold is presented together with the bound substrates thymidine and ATP. Three chain segments at the surface could not be located. The chain fold, the location of the substrates and presumbly also the catalytic mechanism resemble the well-known adenylate kinases.

【 授权许可】

Unknown