Crystal Structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of vibrio cholerae

Rachel Cerdan, Vanessa Bloch, Yinshan Yang, Philippe Bertin, Christian Dumas, Sylvie Rimsky, Michel Kochoyan, Stefan Arold*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

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 2.5Å 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.

Original languageEnglish (US)
Pages (from-to)179-185
Number of pages7
JournalJournal of Molecular Biology
Volume334
Issue number2
DOIs
StatePublished - Nov 21 2003

Keywords

  • DNA-binding protein
  • H-NS protein
  • Vibrio cholerae
  • X-ray structure

ASJC Scopus subject areas

  • Molecular Biology

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