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Crystal structure of a TFIIB–TBP–TATA-element ternary complex

Nature volume 377, pages 119–128 (1995)Cite this article

Abstract

The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element ternary complex is described at 2.7 Å resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the ternary complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

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Author notes

  1. Koji Hisatake

    Present address: Department of Biochemistry, Saitama Medical School, 38 Morohongo, Moroyama, Iruma-gun, Saitama, 350-04, Japan

Authors and Affiliations

  1. Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Dimitar B. Nikolov, Hua Chen, Elaine D. Halay & Stephen K. Burley

  2. Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Koji Hisatake, Dong Kun Lee & Robert G. Roeder

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

    Hua Chen, Elaine D. Halay & Stephen K. Burley

  4. Department of Biology, Princeton University, Princeton, New Jersey, 08544, USA

    Anny A. Usheva

Authors
  1. Dimitar B. Nikolov
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  2. Hua Chen
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Nikolov, D., Chen, H., Halay, E. et al. Crystal structure of a TFIIB–TBP–TATA-element ternary complex. Nature 377, 119–128 (1995). https://doi.org/10.1038/377119a0

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