Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli.
We have directly measured the stoichiometry of maltodextrin-binding sites in LamB. Scatchard plots and computer fitting of flow dialysis (rate-of-dialysis) experiments clearly establish three independent binding sites per LamB trimer, with a dissociation constant of approximately 60 microM for maltoheptaose. The current model for LamB's function as a specific pore is discussed with respect to the symmetry in LamB's kinetic properties and the implications of our results.
Gehring
K
K
Cell and Molecular Biology, Lawrence Berkeley Laboratory, California.
Cheng
C H
CH
Nikaido
H
H
Jap
B K
BK
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001665:Binding Sites; D003956:Dialysis; D004926:Escherichia coli; D007700:Kinetics; D046911:Macromolecular Substances; D011134:Polysaccharides / Q000378:metabolism*; D018272:Porins; D011991:Receptors, Virus / Q000378:metabolism*; D012995:Solubility; D013329:Structure-Activity Relationship
D001425:Bacterial Outer Membrane Proteins; D046911:Macromolecular Substances; D011134:Polysaccharides; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins; C008315:maltodextrin