Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli

FEBS Lett. 1995 Feb 27;360(2):125-31. doi: 10.1016/0014-5793(95)00079-o.

Abstract

The three-dimensional structure of the C-terminal domain (47 residues) obtained from the hydrolysis of H-NS protein with bovine trypsin was determined by NMR measurements and distance geometry calculations. It is composed of an antiparallel beta-sheet, an alpha-helix and a 3(10)-helix which form a hydrophobic core, stabilizing the whole structure. This domain has been found to bind to DNA. Possible DNA binding sites are discussed on the basis of the solution structure of the C-terminal domain of H-NS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / ultrastructure*
  • Bacterial Proteins / ultrastructure*
  • Base Sequence
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / ultrastructure*
  • Escherichia coli / chemistry
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / chemistry
  • Peptide Fragments
  • Protein Structure, Tertiary
  • Solutions

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • DNA-Binding Proteins
  • H-NS protein, bacteria
  • Oligodeoxyribonucleotides
  • Peptide Fragments
  • Solutions