Co-crystal Structure of TBP Recognizing the Minor Groove of a TATA Element

Nature. 1993 Oct 7;365(6446):520-7. doi: 10.1038/365520a0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / genetics
  • Amino Acid Sequence
  • Arabidopsis
  • Base Sequence
  • Binding Sites
  • Computer Graphics
  • Crystallography, X-Ray
  • DNA / chemistry
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Promoter Regions, Genetic
  • Protein Conformation
  • Saccharomyces cerevisiae
  • TATA Box*
  • Transcription Factor TFIID
  • Transcription Factors / chemistry*
  • Transcription, Genetic

Substances

  • Transcription Factor TFIID
  • Transcription Factors
  • DNA