Crystal structure of a human TATA box-binding protein/TATA element complex

Proc Natl Acad Sci U S A. 1996 May 14;93(10):4862-7. doi: 10.1073/pnas.93.10.4862.

Abstract

The TATA box-binding protein (TBP) is required by all three eukaryotic RNA polymerases for correct initiation of transcription of ribosomal, messenger, small nuclear, and transfer RNAs. The cocrystal structure of the C-terminal/core region of human TBP complexed with the TATA element of the adenovirus major late promoter has been determined at 1.9 angstroms resolution. Structural and functional analyses of the protein-DNA complex are presented, with a detailed comparison to our 1.9-angstroms resolution structure of Arabidopsis thaliana TBP2 bound to the same TATA box.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / chemistry
  • Base Sequence
  • Conserved Sequence
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA / genetics
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Nucleic Acid Conformation
  • Plant Proteins / chemistry
  • Protein Conformation
  • TATA Box*
  • TATA-Box Binding Protein
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

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

Associated data

  • PDB/1CDW