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Science 10 May 1996:
Vol. 272. no. 5263, pp. 830 - 836
DOI: 10.1126/science.272.5263.830

Research Articles

Crystal Structure of the Yeast TFIIA/TBP/DNA Complex

James H. Geiger, Steve Hahn, Sally Lee, Paul B. Sigler *

The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was solved to 3 angstrom resolution by double-edge multiple wavelength anomalous diffraction from two different species of anomalous scattering elements in the same crystal. The large and small subunits of TFIIA associate intimately to form both domains of a two-domain folding pattern. TFIIA binds as a heterodimer to the side of the TBP/TATA complex opposite to the side that binds TFIIB and does not alter the TBP/DNA interaction. The six-stranded beta -sandwich domain interacts with the amino-terminal end of TBP through a stereospecific parallel beta -strand interface and with the backbone of the TATA box and the 5'-flanking B-DNA segment. The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions.

J. H. Geiger and P. B. Sigler are in the Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06510, USA. S. Hahn and S. Lee are at the Fred Hutchinson Cancer Research Center, A1-162, Seattle, WA 98104, USA.
* To whom correspondence should be addressed.



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Protease Footprinting Analysis of Ternary Complex Formation by Human TFIIA.
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RNA polymerase II transcription initiation: A structural view.
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B. R. Peterson, L. J. Sun, and G. L. Verdine (1996)
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