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

FEBS Letters

Mizuno, Takeshi⁴  Nakamura, Haruki¹  Ueguchi, Chiharu⁴  Iwaki, Takanobu²  Shindo, Heisaburo²  Kuboniwa, Hitoshi³  Ieda, Ryoichi²  Kurumizaka, Hitoshi²  Morikawa, Soichi¹ 

[1] Protein Engineering Research Institute, Furuedai, Suita 565, Japan;Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Tokyo 192-03, Japan;Chugai Pharmaceutical Inc., Gotenba, Shizuoka 412, Japan;School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464, Japan

关键词: H-NS;    NMR;    Solution structure;    DNA binding protein;   

DOI  :  10.1016/0014-5793(95)00079-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown