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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Cerdan R,Bloch V,Yang Y,Bertin P,Dumas C,Rimsky S,Kochoyan M,Arold ST

doi

10.1016/j.jmb.2003.09.051

keywords:

subject

Has Abstract

pub_date

2003-11-21 00:00:00

pages

179-85

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022283603012051

journal_volume

334

pub_type

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