Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.

@article{Hall2016StructuralBF,
  title={Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.},
  author={Michael J Hall and Christin Grundstr{\"o}m and Afshan Begum and Mikael J Lindberg and Uwe H. Sauer and Fredrik Almqvist and J{\"o}rgen Johansson and A Elisabeth Sauer-Eriksson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 51},
  pages={14733-14738}
}
Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box… CONTINUE READING

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