1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG.
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.
Kim
J L
JL
Laboratory of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.
Burley
S K
SK
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry; D001483:Base Sequence; D001665:Binding Sites; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012997:Solvents / Q000737:chemistry; D016385:TATA Box; D035181:TATA-Box Binding Protein; D014157:Transcription Factors / Q000737:chemistry*
D004268:DNA-Binding Proteins; D012997:Solvents; D035181:TATA-Box Binding Protein; D014157:Transcription Factors; D004247:DNA