5lrs | pdb_00005lrs

The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30-bp operator PrfA-box motif

spinqualitylabelsall models 5lrs, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lrs is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GSH Related: 2beo Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 PrfAWT in complex only with DNA confirms that PrfAWT 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. Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.,Hall M, Grundstrom C, Begum A, Lindberg MJ, Sauer UH, Almqvist F, Johansson J, Sauer-Eriksson AE Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14733-14738. doi:, 10.1073/pnas.1614028114. Epub 2016 Dec 5. PMID:27930316 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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