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

This is the authors' abstract. We don't add key points for this paper.

Significance Infection by the human bacterial pathogen Listeria monocytogenes is controlled mainly by the transcriptional activator PrfA, a member of the Crp/Fnr family. Here we report the crystal structures of PrfA in complex with glutathione (GSH) and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. The structures provide detailed information and insight into how GSH interacts with PrfA and thus induces the correct fold of the HTH motif promoting PrfA DNA binding.