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Co-crystal structure of TBP recognizing the minor groove of a TATA element

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Abstract

The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 Å resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel β-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine–base stacking interactions.

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Authors and Affiliations

  1. Laboratories of Molecular Biophysics and,

    Joseph L. Kim, Dimitar B. Nikolov & Stephen K. Burley

  2. Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Joseph L. Kim & Stephen K. Burley

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  1. Joseph L. Kim
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  2. Dimitar B. Nikolov
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  3. Stephen K. Burley
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Kim, J., Nikolov, D. & Burley, S. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365, 520–527 (1993). https://doi.org/10.1038/365520a0

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