{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wilkening RV"],"funding":["NIAID NIH HHS","Burroughs Wellcome Fund","National Institutes of Health"],"pagination":["20544-20557"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5733591"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["292(50)"],"pubmed_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 <i>Streptococcus dysgalactiae</i> (Rgg2<sub>Sd</sub>). Here, we compared two Rgg2<sub>Sd</sub>(C45S) X-ray crystal structures with that of wild-type Rgg2<sub>Sd</sub> and found that in the absence of the intermolecular disulfide, the Rgg2<sub>Sd</sub> dimer interface is destabilized and Rgg2<sub>Sd</sub> can ado"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Activating mutations in quorum-sensing regulator Rgg2 and its conformational flexibility in the absence of an intermolecular disulfide bond."],"pmcid":["PMC5733591"],"funding_grant_id":["R01 AI091779","R01 AI125452","AI125452","AI091779"],"pubmed_authors":["Neiditch MB","Capodagli GC","Tylor KM","Federle MJ","Khataokar A","Wilkening RV"],"additional_accession":[]},"is_claimable":false,"name":"Activating mutations in quorum-sensing regulator Rgg2 and its conformational flexibility in the absence of an intermolecular disulfide bond.","description":"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 <i>Streptococcus dysgalactiae</i> (Rgg2<sub>Sd</sub>). Here, we compared two Rgg2<sub>Sd</sub>(C45S) X-ray crystal structures with that of wild-type Rgg2<sub>Sd</sub> and found that in the absence of the intermolecular disulfide, the Rgg2<sub>Sd</sub> dimer interface is destabilized and Rgg2<sub>Sd</sub> can ado","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Dec","modification":"2026-05-02T09:17:50.535Z","creation":"2019-03-27T00:11:22Z"},"accession":"S-EPMC5733591","cross_references":{"pubmed":["29030429"],"doi":["10.1074/jbc.m117.801670","10.1074/jbc.M117.801670"]}}