SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF A NUCLEOID-ASSOCIATED PROTEIN, H-NS, FROM ESCHERICHIA-COLI

被引：106

作者：

SHINDO, H

IWAKI, T

IEDA, R

KURUMIZAKA, H

UEGUCHI, C

MIZUNO, T

MORIKAWA, S

NAKAMURA, H

KUBONIWA, H

机构：

[1] NAGOYA UNIV,SCH AGR,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN

[2] PROT ENGN RES INST,SUITA,OSAKA 565,JAPAN

[3] CHUGAI PHARMACEUT CO LTD,GOTEMBA,SHIZUOKA 412,JAPAN

来源：

FEBS LETTERS | 1995年 / 360卷 / 02期

关键词：

H-NS; NMR; SOLUTION STRUCTURE; DNA BINDING PROTEIN;

D O I：

10.1016/0014-5793(95)00079-O

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 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.

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页码：125 / 131

页数：7

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