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2.1 Å resolution refined structure of a TATA box-binding protein (TBP)

Nature Structural Biology volume 1, pages 621–637 (1994)Cite this article

Abstract

The three-dimensional structure of a TATA box-binding protein (TBP2) from Arabidopsis thaliana has been refined at 2.1 Å resolution. TBPs are general eukaryotic transcription factors that participate in initiation of RNA synthesis by all three eukaryotic RNA polymerases. The carboxy-terminal portion of TBP is a unique DNA-binding motif/protein fold, adopting a highly symmetric α/β structure that resembles a molecular saddle with two stirrup-like loops. A ten-stranded, antiparallel β-sheet provides a concave surface for recognizing class II nuclear gene promoters, while the four amphipathic α-helices on the convex surface are available for interaction with other transcription factors. The myriad interactions of TBP2 with components of the transcription machinery are discussed.

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

    Dimitar B. Nikolov

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

    Stephen K. Burley

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Nikolov, D., Burley, S. 2.1 Å resolution refined structure of a TATA box-binding protein (TBP). Nat Struct Mol Biol 1, 621–637 (1994). https://doi.org/10.1038/nsb0994-621

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