1ov9

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spinqualitylabelsall models 1ov9, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1OV9 is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae., Cerdan R, Bloch V, Yang Y, Bertin P, Dumas C, Rimsky S, Kochoyan M, Arold ST, J Mol Biol. 2003 Nov 21;334(2):179-85. PMID:14607110

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