This entry represents the C-terminal domain of the H-NS DNA binding protein. It is composed of an antiparallel beta-sheet, an alpha-helix and a 3 (10)-helix which form a hydrophobic core, stabilising the whole structure. This domain has been found to bind to DNA [ (PUBMED:7875316) ].
Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.
FEBS Lett. 1995; 360: 125-31
Display 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 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.