1LR1

Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS

Summary for 1LR1

• Entry DOI: 10.2210/pdb1lr1/pdb
• Related: 1HNS
• NMR Information: BMRB: 5390
• Descriptor: dna-binding protein h-ns (1 entity in total)
• Functional Keywords: chromatin, coiled-coil, dna packaging, nucleoid assembly, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 14039.80

Authors

Esposito, D.,Petrovic, A.,Harris, R.,Ono, S.,Eccleston, J.,Mbabaali, A.,Haq, I.,Higgins, C.F.,Hinton, J.C.D.,Driscoll, P.C.,Ladbury, J.E. (deposition date: 2002-05-14, release date: 2003-01-14, Last modification date: 2024-05-22)

Primary citation

Esposito, D.,Petrovic, A.,Harris, R.,Ono, S.,Eccleston, J.,Mbabaali, A.,Haq, I.,Higgins, C.F.,Hinton, J.C.,Driscoll, P.C.,Ladbury, J.E.
H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein
J.Mol.Biol., 324:841-850, 2002

PubMed Abstract: H-NS plays a role in condensing DNA in the bacterial nucleoid. This 136 amino acid protein comprises two functional domains separated by a flexible linker. High order structures formed by the N-terminal oligomerization domain (residues 1-89) constitute the basis of a protein scaffold that binds DNA via the C-terminal domain. Deletion of residues 57-89 or 64-89 of the oligomerization domain precludes high order structure formation, yielding a discrete dimer. This dimerization event represents the initial event in the formation of high order structure. The dimers thus constitute the basic building block of the protein scaffold. The three-dimensional solution structure of one of these units (residues 1-57) has been determined. Activity of these structural units is demonstrated by a dominant negative effect on high order structure formation on addition to the full length protein. Truncated and site-directed mutant forms of the N-terminal domain of H-NS reveal how the dimeric unit self-associates in a head-to-tail manner and demonstrate the importance of secondary structure in this interaction to form high order structures. A model is presented for the structural basis for DNA packaging in bacterial cells.

PubMed: 12460581
DOI: 10.1016/S0022-2836(02)01141-5

Experimental method

SOLUTION NMR