1OV9

Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae

Summary for 1OV9

• Entry DOI: 10.2210/pdb1ov9/pdb
• Related: 1LR1 1NI8
• Descriptor: VicH protein (2 entities in total)
• Functional Keywords: dimer, helix, coiled-coil, dna binding protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 2
• Total formula weight: 11503.00

Authors

Cerdan, R.,Bloch, V.,Arold, S.T. (deposition date: 2003-03-26, release date: 2003-11-25, Last modification date: 2023-08-16)

Primary citation

Cerdan, R.,Bloch, V.,Yang, Y.,Bertin, P.,Dumas, C.,Rimsky, S.,Kochoyan, M.,Arold, S.T.
The Crystal Structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio Cholerae
J.Mol.Biol., 334:179-185, 2003

PubMed Abstract: The histone-like nucleoid structuring (H-NS) protein is a global modulator of gene expression in Gram-negative bacteria. VicH, the H-NS protein of Vibrio cholerae, regulates the expression of certain major virulence determinants implicated in the pathogenesis of cholera. We present here the 2.5A crystal structure of the N-terminal oligomerisation domain of VicH (VicH_Nt). VicH_Nt adopts the same fold and dimeric assembly as the NMR structure of Escherichia coli H-NS_Nt, thus validating this fold against conflicting data. The structural similarity of V.cholerae VicH_Nt and E.coli H-NS_Nt, despite differences in origin, system of expression, experimental conditions and techniques used, indicates that the fold determined in our studies is robust to experimental conditions. Structural analysis and homology modelling were carried out to further elucidate the molecular basis of the functional polyvalence of the N-terminal domain. Our analysis of members of the H-NS superfamily supports the suggestion that the oligomerisation function of H-NS_Nt is conserved even in more distantly related proteins.

PubMed: 14607110
DOI: 10.1016/j.jmb.2003.09.051

Experimental method

X-RAY DIFFRACTION (2.3 Å)