The three-dimensional structure of thymidine kinase from herpes simplex virus type 1.
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.
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Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.
Bohner
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Aubry
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Folkers
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Schulz
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D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013937:Thymidine Kinase / Q000737:chemistry*
D011993:Recombinant Fusion Proteins; D013937:Thymidine Kinase