Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

Nature. 1993 Mar 18;362(6417):219-23. doi: 10.1038/362219a0.

Abstract

The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 A resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein. The structure shows a striking similarity to the DNA-binding domain of the catabolite gene activator protein CAP, thereby providing a possible model for the binding of GH5 to DNA.

Publication types

  • Comparative Study
  • 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
  • Cloning, Molecular
  • Cyclic AMP Receptor Protein / chemistry
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • Escherichia coli / genetics
  • Histones / chemistry*
  • Histones / genetics
  • Histones / metabolism*
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleosomes / metabolism*
  • Protein Structure, Secondary*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • X-Ray Diffraction / methods

Substances

  • Cyclic AMP Receptor Protein
  • DNA-Binding Proteins
  • Histones
  • Nucleosomes
  • Recombinant Proteins
  • DNA