Crystal structure of Campylobacter jejuni peroxide regulator

FEBS Lett. 2018 Jul;592(13):2351-2360. doi: 10.1002/1873-3468.13120. Epub 2018 Jun 14.


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.

Keywords: PerR; metal regulation; transcription.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Campylobacter jejuni* / genetics
  • Campylobacter jejuni* / metabolism
  • Campylobacter jejuni* / pathogenicity
  • Crystallography, X-Ray
  • Escherichia coli
  • Gene Expression Regulation, Bacterial
  • Models, Molecular
  • Oxidation-Reduction
  • Oxidative Stress / genetics
  • Peroxides / chemistry
  • Peroxides / metabolism
  • Protein Conformation, alpha-Helical
  • Reactive Oxygen Species / metabolism
  • Repressor Proteins / chemistry*
  • Repressor Proteins / metabolism
  • Sequence Homology
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism


  • Bacterial Proteins
  • Peroxides
  • Reactive Oxygen Species
  • Repressor Proteins
  • Transcription Factors
  • peroxide repressor proteins