The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was
solved to 3 angstrom resolution by double-edge multiple wavelength an
omalous diffraction from two different species of anomalous scattering
elements in the same crystal. The large and small subunits of TFIIA a
ssociate intimately to form both domains of a two-domain folding patte
rn. TFIIA binds as a heterodimer to the side of the TBP/TATA complex o
pposite to the side that binds TFIIB and does not alter the TBP/DNA in
teraction. The six-stranded beta-sandwich domain interacts with the am
ino-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/T
ATA complex, thereby presenting a substantial surface for further prot
ein-protein interactions.