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

*この研究の対応する著者

研究成果: Article査読

99 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)125-131
ページ数7
ジャーナルFEBS Letters
360
2
DOI
出版ステータスPublished - 1995 2月 27
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 生物理学
  • 細胞生物学
  • 遺伝学
  • 分子生物学
  • 構造生物学

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