2015
Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*
Tavoulari S, Margheritis E, Nagarajan A, DeWitt DC, Zhang YW, Rosado E, Ravera S, Rhoades E, Forrest LR, Rudnick G. Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*. Journal Of Biological Chemistry 2015, 291: 1456-1471. PMID: 26582198, PMCID: PMC4714228, DOI: 10.1074/jbc.m115.692012.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAmino Acid Transport SystemsAquatic OrganismsBacterial ProteinsBinding SitesCysteineGram-Negative BacteriaLigandsLiposomesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationPlasma Membrane Neurotransmitter Transport ProteinsProtein ConformationProtein FoldingProtein StabilityProteolipidsRecombinant ProteinsSodiumConceptsConformational changesTransmembrane helix 1Open conformational stateDependent conformational changesTransporter homologExtracellular gateProkaryotic homologCytoplasmic pathwayHelix 1Interaction networksIntermediary interactionsBiophysical assaysNeurotransmitter transportersSubstrate pathwayNa2 siteConformational statesHelix motionsLeuTDirect interactionDependent closureHomologMutantsDistinct stepsResiduesComputational analysis
2010
Reconstructing a Chloride-binding Site in a Bacterial Neurotransmitter Transporter Homologue*
Tavoulari S, Rizwan AN, Forrest LR, Rudnick G. Reconstructing a Chloride-binding Site in a Bacterial Neurotransmitter Transporter Homologue*. Journal Of Biological Chemistry 2010, 286: 2834-2842. PMID: 21115480, PMCID: PMC3024779, DOI: 10.1074/jbc.m110.186064.Peer-Reviewed Original ResearchConceptsChloride-binding siteConformational changesAdjacent binding sitesSingle point mutationProkaryotic homologuesSubstrate translocationIon-binding sitesTransporter homologueTransport proteinsNeurotransmitter transportersNeurotransmitter transportPoint mutationsBinding sitesHomologuesProteinMutationsCl(-) bindsDirect evidenceTherapeutic drugsSitesDependent formTranslocationTransportersBindsResidues
1976
Equilibrium between two forms of the lac carrier protein in energized and nonenergized membrane vesicles from Escherichia coli.
Rudnick G, Schuldiner S, Kaback H. Equilibrium between two forms of the lac carrier protein in energized and nonenergized membrane vesicles from Escherichia coli. Biochemistry 1976, 15: 5126-31. PMID: 791364, DOI: 10.1021/bi00668a028.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesBiological TransportCell MembraneDinitrophenolsEscherichia coliGalactosidesKineticsLactoseNitrophenolsConceptsLac carrier proteinMembrane vesiclesCarrier proteinY gene productEscherichia coli ML 308P-nitrophenyl alphaD-lactateMembrane proteinsGene productsML 308Cryptic formVesicle membraneLactose transportElectrochemical gradientEscherichia coliEnergy couplingProteinVesiclesCarbonyl cyanideSimilar affinityCompetitive inhibitorHigh affinity formMembraneBindingFlow dialysis