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 A
resolution, giving a final crystallographic R-factor of 19.4%. Binding of the
monomeric, saddle-shaped alpha/beta 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.