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Active transport by customized β–barrels

Nature Structural Biology volume 6, pages 3–6 (1999)Cite this article

Abstract

The crystal structures of two bacterial outer membrane transport proteins — FepA and FhuA — put the field on a solid molecular foundation and suggest an exciting and novel active transport mechanism.

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Figure 1: A simplified model for the TonB–dependent energy transduction cycle.
Figure 2: Ribbon diagram of FepA.
Figure 3: Topology of the FepA barrel, using amino acid sequence in one–letter code.

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  1. the Departments of Microbiology and Biochemistry/Biophysics, Washington State University, Pullman , 99164–4233, Washington, USA

    Kathleen Postle

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  1. Kathleen Postle
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Postle, K. Active transport by customized β–barrels. Nat Struct Mol Biol 6, 3–6 (1999). https://doi.org/10.1038/4869

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