Crystal structure of the DNA binding domain of the heat shock transcription factor

Science. 1994 Jan 14;263(5144):224-7. doi: 10.1126/science.8284672.

Abstract

The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins*
  • Helix-Loop-Helix Motifs*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Transcription Factors / chemistry*

Substances

  • DNA-Binding Proteins
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins
  • Transcription Factors
  • DNA