Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.
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.
Shindo
H
H
Tokyo University of Pharmacy and Life Science, Japan.
Iwaki
T
T
Ieda
R
R
Kurumizaka
H
H
Ueguchi
C
C
Mizuno
T
T
Morikawa
S
S
Nakamura
H
H
Kuboniwa
H
H
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure*; D001426:Bacterial Proteins / Q000648:ultrastructure*; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D004926:Escherichia coli / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010446:Peptide Fragments; D017434:Protein Structure, Tertiary; D012996:Solutions
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D009838:Oligodeoxyribonucleotides; D010446:Peptide Fragments; D012996:Solutions