The 2.5 angstrom crystal structure of a TATA-box complex with yeast TB
P shows that the eight base pairs of the TATA box bind to the concave
surface of TBP by bending towards the major groove with unprecedented
severity. This produces a wide open, underwound, shallow minor groove
which forms a primarily hydrophobic interface with the entire under-su
rface of the TBP saddle. The severe bend and a positive writhe radical
ly alter the trajectory of the flanking B-form DNA.