The Journal of Membrane Biology

, Volume 100, Issue 1, pp 21–29 | Cite as

Mechanism of sugar transport through the sugar-specific LamB channel ofEscherichia coli outer membrane

  • Roland Benz
  • Angela Schmid
  • Greetje H. Vos-Scheperkeuter
Article

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. USA77:165–171 (1980a)) and the stability constants for the sugar binding given in this study.

Key Words

LamB maltoporin lipid bilayer sugar transport transport mechanism membrane channel 

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Copyright information

© Springer-Verlag New York Inc. 1987

Authors and Affiliations

  • Roland Benz
    • 1
  • Angela Schmid
    • 1
  • Greetje H. Vos-Scheperkeuter
    • 2
  1. 1.Lehrstuhl für Biotechnologie der Universität WürzburgWürzburgFederal Republic of Germany
  2. 2.Laboratory of BiochemistryState University of GroningenGroningenThe Netherlands

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