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

doi:10.1016/0014-5793(95)00079-O

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

100 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 language	English
Pages (from-to)	125-131
Number of pages	7
Journal	FEBS Letters
Volume	360
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(95)00079-O
Publication status	Published - 1995 Feb 27
Externally published	Yes

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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10.1016/0014-5793(95)00079-O

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

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.",

keywords = "DNA binding protein, H-NS, NMR, Solution structure",

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

year = "1995",

month = feb,

day = "27",

doi = "10.1016/0014-5793(95)00079-O",

language = "English",

volume = "360",

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journal = "FEBS Letters",

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TY - JOUR

T1 - Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli

AU - Shindo, Heisaburo

AU - Iwaki, Takanobu

AU - Ieda, Ryoichi

AU - Kurumizaka, Hitoshi

AU - Ueguchi, Chiharu

AU - Mizuno, Takeshi

AU - Morikawa, Soichi

AU - Nakamura, Haruki

AU - Kuboniwa, Hitoshi

PY - 1995/2/27

Y1 - 1995/2/27

N2 - 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.

AB - 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.

KW - DNA binding protein

KW - H-NS

KW - NMR

KW - Solution structure

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DO - 10.1016/0014-5793(95)00079-O

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VL - 360

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EP - 131

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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