Crystal structure of a yeast TFIIA/TBP/DNA complex

Nature. 1996 May 9;381(6578):127-51. doi: 10.1038/381127a0.

Abstract

The X-ray crystal structure of the transcription factor IIA (TFIIA) in complex with the TATA-box-binding protein (TBP) and TATA-element DNA is presented at 2.5 A resolution. TFIIA is composed of a beta-barrel and a four-helix bundle motif that together have a boot-like appearance. The beta-barrel extends the TBP beta-sheet and bridges over the DNA major groove immediately upstream of the TATA box. The four-helix bundle contributes substantially to the surface of the complex available for interaction with additional transcription factors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Crystallography, X-Ray
  • Cytochrome c Group / genetics
  • Cytochromes c*
  • DNA, Fungal / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins*
  • TATA Box
  • TATA-Box Binding Protein
  • Transcription Factor TFIIA
  • Transcription Factors / chemistry*
  • Transcription, Genetic

Substances

  • CYC1 protein, S cerevisiae
  • Cytochrome c Group
  • DNA, Fungal
  • DNA-Binding Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • TATA-Box Binding Protein
  • Transcription Factor TFIIA
  • Transcription Factors
  • Cytochromes c