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  • Title: Periplasmic maltose-binding protein confers specificity on the outer membrane maltose pore of Escherichia coli.
    Author: Heuzenroeder MW, Reeves P.
    Journal: J Bacteriol; 1980 Feb; 141(2):431-5. PubMed ID: 6444941.
    Abstract:
    ompB mutants of Escherichia coli K-12 are markedly deficient in porin in their outer membrane. This results in a decreased rate of uptake for many substrates: the maltose pore (lambda receptor) can in some circumstances, in the absence of the periplasmic maltose-binding protein, compensate for the consequent defects in permeability to lactose, mannitol, glycylglycyl-L-valine, and tri-L-ornithine. It is postulated that the maltose-binding protein associates with the maltose pore and confers on it the specificity for maltose, and that the absence of the maltose-binding protein leaves the pore open and results in enhanced transmembrane diffusion of molecules other than maltose. This paper presents evidence to support this hypothesis.
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