Wild K, Bohner T, Aubry A, Folkers G, Schulz G E
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.
FEBS Lett. 1995 Jul 17;368(2):289-92. doi: 10.1016/0014-5793(95)00680-8.
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 A 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.
来自1型单纯疱疹病毒的重组胸苷激酶（ATP：胸苷5'-磷酸转移酶；EC 2.7.1.21）是一种具有治疗重要性的酶，以N端截短但仍具有完全活性的形式被纯化并结晶。通过使用同晶置换法在3.0埃分辨率下进行X射线衍射分析确定了其三维结构。展示了链折叠以及结合的底物胸苷和ATP。表面的三个链段无法定位。链折叠、底物的位置以及推测的催化机制类似于著名的腺苷酸激酶。
