Allosteric regulation of the glucose:H+ symporter of Lactobacillus brevis: cooperative binding of glucose and HPr(ser-P).
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.
Ye
J J
JJ
Department of Biology, University of California at San Diego, La Jolla 92093-0116.
Saier
M H
MH
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
D001426:Bacterial Proteins; D009004:Monosaccharide Transport Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; C031629:phosphoenolpyruvate-glucose phosphotransferase; D005947:Glucose