Activating mutations in quorum-sensing regulator Rgg2 and its conformational flexibility in the absence of an intermolecular disulfide bond.

ABSTRACT: Rap/Rgg/NprR/PlcR/PrgX (RRNPP) quorum-sensing systems use extracellular peptide pheromones that are detected by cytoplasmic receptors to regulate gene expression in firmicute bacteria. Rgg-type receptors are allosterically regulated through direct pheromone binding to control transcriptional activity; however, the receptor activation mechanism remains poorly understood. Previous work has identified a disulfide bond between Cys-45 residues within the homodimer interface of Rgg2 from Streptococcus dysgalactiae (Rgg2_Sd). Here, we compared two Rgg2_Sd(C45S) X-ray crystal structures with that of wild-type Rgg2_Sd and found that in the absence of the intermolecular disulfide, the Rgg2_Sd dimer interface is destabilized and Rgg2_Sd can ado

SUBMITTER: Wilkening RV 

PROVIDER: S-EPMC5733591 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature