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1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Nature Structural Biology volume 1, pages 638–653 (1994)Cite this article

Abstract

The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 Å resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped α/β protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly.

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  1. Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY, 10021, USA

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Kim, J., Burley, S. 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG. Nat Struct Mol Biol 1, 638–653 (1994). https://doi.org/10.1038/nsb0994-638

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