1HNS
H-NS (DNA-BINDING DOMAIN)
Summary for 1HNS
| Entry DOI | 10.2210/pdb1hns/pdb |
| Descriptor | H-NS (1 entity in total) |
| Functional Keywords | histone-like protein h1, dna-binding protein, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 5308.93 |
| Authors | Shindo, H.,Iwaki, T.,Ieda, R.,Kurumizaka, H.,Ueguchi, C.,Mizuno, T.,Morikawa, S.,Nakamura, H.,Kuboniwa, H. (deposition date: 1995-04-06, release date: 1995-07-10, Last modification date: 2024-05-22) |
| Primary citation | Shindo, H.,Iwaki, T.,Ieda, R.,Kurumizaka, H.,Ueguchi, C.,Mizuno, T.,Morikawa, S.,Nakamura, H.,Kuboniwa, H. Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Lett., 360:125-131, 1995 Cited by PubMed 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. PubMed: 7875316DOI: 10.1016/0014-5793(95)00079-O PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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