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Science 10 May 1996: Vol. 272. no. 5263, pp. 830 - 836 DOI: 10.1126/science.272.5263.830
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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 -sandwich domain interacts with the
amino-terminal end of TBP through a stereospecific parallel -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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272, 1180-1187
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- The Stability of the TFIIA-TBP-DNA Complex Is Dependent on the Sequence of the TATAAA Element.
- J. J. Stewart and L. A. Stargell (2001)
J. Biol. Chem.
276, 30078-30084
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- Fluorescence-based Analyses of the Effects of Full-length Recombinant TAF130p on the Interaction of TATA Box-binding Protein with TATA Box DNA.
- U. Banik, J. M. Beechem, E. Klebanow, S. Schroeder, and P. A. Weil (2001)
J. Biol. Chem.
276, 49100-49109
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