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

Heisaburo Shindo, Takanobu Iwaki, Ryoichi Ieda, Hitoshi Kurumizaka, Chiharu Ueguchi, Takeshi Mizuno, Soichi Morikawa, Haruki Nakamura, Hitoshi Kuboniwa

Research output: Contribution to journalArticle

92 Citations (Scopus)

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 β-sheet, an α-helix and a 310-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.

Original languageEnglish
Pages (from-to)125-131
Number of pages7
JournalFEBS Letters
Volume360
Issue number2
DOIs
Publication statusPublished - 1995 Feb 27
Externally publishedYes

Keywords

  • DNA binding protein
  • H-NS
  • NMR
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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  • Cite this

    Shindo, H., Iwaki, T., Ieda, R., Kurumizaka, H., Ueguchi, C., Mizuno, T., Morikawa, S., Nakamura, H., & Kuboniwa, H. (1995). Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Letters, 360(2), 125-131. https://doi.org/10.1016/0014-5793(95)00079-O