title: Allosteric regulation of the glucose:H+ symporter of Lactobacillus brevis: cooperative binding of glucose and HPr(ser-P).
abstract: Lactobacillus brevis transports glucose and the nonmetabolizable glucose analog 2-deoxyglucose via a proton symport mechanism that is allosterically inhibited by the seryl-phosphorylated derivative of HPr, the small phosphocarrier protein of the phosphotransferase system. We have demonstrate that S46DHPr, a mutant analog of HPr which conformationally resembles HPr(ser-P) but not free HPr, specifically binds to membranes derived from glucose-grown L. brevis cells if and only if a substrate of the glucose permease is also present.
authors.affiliation: Department of Biology, University of California at San Diego, La Jolla 92093-0116.
authors.forename: J J
authors.initials: JJ
authors.lastname: Ye
authors.forename: M H
authors.initials: MH
authors.lastname: Saier
mesh_terms: D000494:Allosteric Regulation; D001426:Bacterial Proteins; D005947:Glucose / Q000378:metabolism*; D007778:Lactobacillus / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins / Q000502:physiology*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism* / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D009004:Monosaccharide Transport Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; C031629:phosphoenolpyruvate-glucose phosphotransferase; D005947:Glucose