Co-crystal structure of TBP recognizing the minor groove of a TATA element.
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 A resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel beta-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions.
Kim
J L
JL
Laboratory of Molecular Biophysics, Rockefeller University, New York, New York 10021.
Nikolov
D B
DB
Burley
S K
SK
D000256:Adenoviridae / Q000235:genetics; D000595:Amino Acid Sequence; D017360:Arabidopsis; D001483:Base Sequence; D001665:Binding Sites; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae; D016385:TATA Box; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry*; D014158:Transcription, Genetic
D035362:Transcription Factor TFIID; D014157:Transcription Factors; D004247:DNA