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Title
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The three-dimensional structure of thymidine kinase from herpes simplex virus type 1.
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Authors
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K.Wild,
T.Bohner,
A.Aubry,
G.Folkers,
G.E.Schulz.
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Ref.
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FEBS Lett, 1995,
368,
289-292.
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PubMed id
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Abstract
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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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