2018
Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT
Zhang YW, Tavoulari S, Sinning S, Aleksandrova AA, Forrest LR, Rudnick G. Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e8854-e8862. PMID: 30181291, PMCID: PMC6156673, DOI: 10.1073/pnas.1716870115.Peer-Reviewed Original ResearchConceptsTransporter domainConformational changesOpen stateSodium symporter familyIon-substrate couplingTransmembrane ion gradientsSymporter familyNSS transportersSubstrate bindingLeuTIntracellular substratesCysteine accessibilitySubstrate transportAccessibility of substrateTyrosine residuesConformational responseNa2 siteUncoupled movementIon gradientsExtracellular pathwaysMechanistic componentsTransportersProteinTransport of ionsBinding
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 ResearchConceptsLac 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
1975
ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN
Kaback H, Rudnick G, Schuldiner S, Short S. ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN. Annals Of The New York Academy Of Sciences 1975, 264: 350-357. PMID: 769642, DOI: 10.1111/j.1749-6632.1975.tb31495.x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPhotoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with an impermeant azidophenylgalactoside.
Rudnick G, Kaback H. Photoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with an impermeant azidophenylgalactoside. Journal Of Biological Chemistry 1975, 250: 6847-6851. PMID: 1099095, DOI: 10.1016/s0021-9258(19)41009-0.Peer-Reviewed Original ResearchPhotoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with 2-nitro-4-azidophenyl-1-thio-beta-D-galactopyranoside.
Rudnick G, Kaback H, Weil R. Photoinactivation of the beta-galactoside transport system in Escherichia coli membrane vesicles with 2-nitro-4-azidophenyl-1-thio-beta-D-galactopyranoside. Journal Of Biological Chemistry 1975, 250: 1371-1375. PMID: 1089657, DOI: 10.1016/s0021-9258(19)41823-1.Peer-Reviewed Original ResearchConceptsMembrane vesiclesBeta-galactoside transport systemEscherichia coli membrane vesiclesEscherichia coli ML 308Lac carrier proteinD-lactateAmino acid transportTransport systemSteady-state levelsML 308Lactose transportAcid transportCarrier proteinVesiclesD-galactopyranosideApparent KmCompetitive inhibitor