Crystal structure of a TFIIB-TBP-TATA-element ternary complex

Nature. 1995 Sep 14;377(6545):119-28. doi: 10.1038/377119a0.


The crystal structure of the transcription factor IIB (TFIIB)/TATA box-binding protein (TBP)/TATA-element ternary complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP-DNA complex through protein-protein and protein-DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the ternary complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenoviridae / genetics
  • Amino Acid Sequence
  • Arabidopsis
  • Base Sequence
  • Crystallography, X-Ray
  • DNA
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Promoter Regions, Genetic
  • Protein Binding
  • Protein Conformation
  • Recombinant Proteins
  • TATA Box*
  • TATA-Box Binding Protein
  • Transcription Factor TFIIB
  • Transcription Factors / chemistry*
  • Transcriptional Activation


  • DNA-Binding Proteins
  • Recombinant Proteins
  • TATA-Box Binding Protein
  • Transcription Factor TFIIB
  • Transcription Factors
  • DNA