5LRR

The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione

Summary for 5LRR

• Entry DOI: 10.2210/pdb5lrr/pdb
• Related: 2beo
• Descriptor: Listeriolysin positive regulatory factor A, GLUTATHIONE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: transcription regulator, dna binding, activation, glutathione, listeria monocytogenes, transcription, dna binding protein
• Biological source: Listeria monocytogenes
• Total number of polymer chains: 8
• Total formula weight: 221496.60

Authors

Hall, M.,Grundstrom, C.,Begum, A.,Lindberg, M.,Sauer, U.H.,Almqvist, F.,Johansson, J.,Sauer-Eriksson, A.E. (deposition date: 2016-08-19, release date: 2016-12-07, Last modification date: 2024-01-17)

Primary citation

Hall, M.,Grundstrom, C.,Begum, A.,Lindberg, M.J.,Sauer, U.H.,Almqvist, F.,Johansson, J.,Sauer-Eriksson, A.E.
Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.
Proc. Natl. Acad. Sci. U.S.A., 113:14733-14738, 2016

PubMed Abstract: 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 motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfA in complex only with DNA confirms that PrfA can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction.

PubMed: 27930316
DOI: 10.1073/pnas.1614028114

Experimental method

X-RAY DIFFRACTION (2.171 Å)