Crystal structure of Campylobacter jejuni peroxide regulator

Sabina Sarvan, François Charih, James Butcher, Joseph S. Brunzelle, Alain Stintzi, Jean François Couture*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

In Campylobacter jejuni (Cj), the metal-cofactored peroxide response regulator (PerR) transcription factor allows C. jejuni to respond to oxidative stresses. The crystal structure of the metalated form of CjPerR shows that the protein folds as an asymmetric dimer displaying structural differences in the orientation of its DNA-binding domain. Comparative analysis shows that such asymmetry is a conserved feature among crystallized PerR proteins, and mutational analysis reveals that residues found in the first α-helix of CjPerR contribute to DNA binding. These studies present the structure of CjPerR protein and highlight structural heterogeneity in the orientation of the metalated PerR DNA-binding domain which may underlie the ability of PerR to recognize DNA, control gene expression, and contribute to bacterial pathogenesis.

Original languageEnglish (US)
Pages (from-to)2351-2360
Number of pages10
JournalFEBS Letters
Volume592
Issue number13
DOIs
StatePublished - Jul 2018

Keywords

  • PerR
  • metal regulation
  • transcription

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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