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Crystal structure of TFIID TATA-box binding protein

Nature volume 360, pages 40–46 (1992)Cite this article

Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 Å resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

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Author notes

  1. Shu-Hong Hu

    Present address: St Vincent's Institute of Medical Research, Fitzroy, Victoria, 3065, Australia

  2. Judith Lin

    Present address: Department of Medicine, University of Southern California Medical Center, Los Angeles, California, 90033-1084, USA

Authors and Affiliations

  1. Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York, 10021-6399, USA

    Dimitar B. Nikolov, Shu-Hong Hu, Judith Lin & Stephen K. Burley

  2. Laboratory of Plant Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York, 10021-6399, USA

    Alexander Gasch & Nam-Hai Chua

  3. Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York, 10021-6399, USA

    Alexander Hoffmann, Masami Horikoshi & Robert G. Roeder

  4. Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021-6399, USA

    Shu-Hong Hu, Judith Lin & Stephen K. Burley

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Nikolov, D., Hu, SH., Lin, J. et al. Crystal structure of TFIID TATA-box binding protein. Nature 360, 40–46 (1992). https://doi.org/10.1038/360040a0

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