Bacteriophage lambda receptor protein in Escherichia coli K-12: lowered affinity of some mutant proteins for maltose-binding protein in vitro.
Mutant and wild-type LamB proteins (phage lambda receptor proteins) were purified by affinity chromatography with immobilized maltose-binding protein, and their transport functions were tested in reconstituted liposomes. Two mutant proteins exhibited a marked decrease in affinity for immobilized maltose-binding protein, as well as altered transport rates.
D018528:ATP-Binding Cassette Transporters; D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda / Q000378:metabolism*; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000032:analysis*; D029968:Escherichia coli Proteins; D007700:Kinetics; D008081:Liposomes / Q000378:metabolism; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D018272:Porins; D011991:Receptors, Virus / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008081:Liposomes; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins; C461599:maltose transport system, E coli