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Mechanism of sugar transport through the sugar-specific LamB channel ofEscherichia coli outer membrane
Authors:Roland Benz  Angela Schmid  Greetje H Vos-Scheperkeuter
Institution:(1) Lehrstuhl für Biotechnologie der Universität Würzburg, D-8700 Würzburg, Federal Republic of Germany;(2) Laboratory of Biochemistry, State University of Groningen, NL-9747 AG Groningen, The Netherlands
Abstract:Summary Lipid bilayer experiments were performed with the sugar-specific LamB (maltoporin) channel ofEscherichia coli outer membrane. Single-channel analysis of the conductance steps caused by LamB showed that there was a linear relationship between the salt concentration in the aqueous phase and the channel conductance, indicating only small or no binding between the ions and the channel interior. The total or the partial blockage of the ion movement through the LamB channel was not dependent on the ion concentration in the aqueous phase. Both results allowed the investigation of the sugar binding in more detail, and the stability constants of the binding of a large variety of sugars to the binding site inside the channel were calculated from titration experiments of the membrane conductance with the sugars. The channel was highly cation selective, both in the presence and absence of sugars, which may be explained by the existence of carbonyl groups inside the channel. These carbonyl groups may also be involved in the sugar binding via hydrogen bonds. The kinetics of the sugar transport through the LamB channel were estimated relative to maltose by assuming a simple one-site, two-barrier model from the relative rates of permeation taken from M. Luckey and H. Nikaido (Proc. Natl. Acad. Sci. USA 77:165–171 (1980a)) and the stability constants for the sugar binding given in this study.
Keywords:LamB  maltoporin  lipid bilayer  sugar transport  transport mechanism  membrane channel
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