1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Nat Struct Biol. 1994 Sep;1(9):638-53. doi: 10.1038/nsb0994-638.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / chemistry
  • Base Sequence
  • Binding Sites
  • Computer Graphics
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA-Binding Proteins / chemistry*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Solvents / chemistry
  • TATA Box*
  • TATA-Box Binding Protein
  • Transcription Factors / chemistry*

Substances

  • DNA-Binding Proteins
  • Solvents
  • TATA-Box Binding Protein
  • Transcription Factors
  • DNA