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Solution structure of the DNA binding domain of a nucleoid‐associated protein, H‐NS, from Escherichia coli
Author(s) -
Shindo Heisaburo,
Iwaki Takanobu,
Ieda Ryoichi,
Kurumizaka Hitoshi,
Ueguchi Chiharu,
Mizuno Takeshi,
Morikawa Soichi,
Nakamura Haruki,
Kuboniwa Hitoshi
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00079-o
Subject(s) - antiparallel (mathematics) , nucleoid , crystallography , b3 domain , dna , chemistry , dna binding domain , helix (gastropod) , escherichia coli , protein structure , binding domain , alpha helix , protein secondary structure , domain (mathematical analysis) , biophysics , stereochemistry , binding site , biochemistry , circular dichroism , biology , physics , transcription factor , ecology , mathematical analysis , mathematics , quantum mechanics , snail , magnetic field , gene
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 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.