THE 3-DIMENSIONAL STRUCTURE OF THYMIDINE KINASE FROM HERPES-SIMPLEX VIRUS TYPE-1

Recombinant thymidine kinase from Herpes simplex virus type 1 (ATP:thy midine 5'-phosphotransferase; EC 2.7.1.21), an enzyme of therapeutic i mportance, was purified and crystallized in an N-terminally truncated but still fully active form. The three-dimensional structure was solve d by X-ray diffraction analysis at 3.0 Angstrom resolution using isomo rphous replacement. The chain fold is presented together with the boun d substrates thymidine acid ATP. Three chain segments at the surface c ould not be located, The chain fold, the location of the substrates an d presumbly also the catalytic mechanism resemble the well-known adeny late kinases.