Transmembrane passage of hydrophobic compounds through a protein channel wall

Elizabeth M. Hearn, Dimki R. Patel, Bryan W. Lepore, Mridhu Indic and Bert van den Berg ()
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Elizabeth M. Hearn: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
Dimki R. Patel: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
Bryan W. Lepore: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
Mridhu Indic: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
Bert van den Berg: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA

Nature, 2009, vol. 458, issue 7236, 367-370

Abstract: Transmembrane transport of hydrophobic compounds Hydrophobic compounds are transported both into and out of cells. Because of the lipophilic nature of hydrophobic compounds, it is thought that such substrates enter efflux pumps by lateral diffusion from the lipid bilayer. Here, Hearn and colleagues present the structure of an Escherichia coli long-chain fatty acid importer, FadL, which reveals an opening in the wall of its transmembrane β-barrel. They further show that a mutant in which this opening is constricted is unable to transport substrate. They conclude that importers, like exporters, may exploit lateral diffusion for the transport of hydrophobic substrates.

Date: 2009
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DOI: 10.1038/nature07678

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