3NR7

Crystal structure of S. typhimurium H-NS 1-83

Summary for 3NR7

• Entry DOI: 10.2210/pdb3nr7/pdb
• Descriptor: DNA-binding protein H-NS (1 entity in total)
• Functional Keywords: dimer, oligomerisation, dna condensation, dna binding protein
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 2
• Total formula weight: 19592.10

Authors

Arold, S.T.,Leonard, P.G.,Parkinson, G.N.,Ladbury, J.E. (deposition date: 2010-06-30, release date: 2010-09-01, Last modification date: 2023-09-06)

Primary citation

Arold, S.T.,Leonard, P.G.,Parkinson, G.N.,Ladbury, J.E.
H-NS forms a superhelical protein scaffold for DNA condensation.
Proc.Natl.Acad.Sci.USA, 107:15728-15732, 2010

PubMed Abstract: The histone-like nucleoid structuring (H-NS) protein plays a fundamental role in DNA condensation and is a key regulator of enterobacterial gene expression in response to changes in osmolarity, pH, and temperature. The protein is capable of high-order self-association via interactions of its oligomerization domain. Using crystallography, we have solved the structure of this complete domain in an oligomerized state. The observed superhelical structure establishes a mechanism for the self-association of H-NS via both an N-terminal antiparallel coiled-coil and a second, hitherto unidentified, helix-turn-helix dimerization interface at the C-terminal end of the oligomerization domain. The helical scaffold suggests the formation of a H-NS:plectonemic DNA nucleoprotein complex that is capable of explaining published biophysical and functional data, and establishes a unifying structural basis for coordinating the DNA packaging and transcription repression functions of H-NS.

PubMed: 20798056
DOI: 10.1073/pnas.1006966107

Experimental method

X-RAY DIFFRACTION (3.7 Å)