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Structural basis of Na+-independent and cooperative substrate/product antiport in CaiT

Author

Listed:
  • Sabrina Schulze

    (Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany)

  • Stefan Köster

    (Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany)

  • Ulrike Geldmacher

    (Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany)

  • Anke C. Terwisscha van Scheltinga

    (Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany
    Present address: Laboratory of Biophysical Chemistry, Nijenborgh 4, 9747 AG Groningen, The Netherlands.)

  • Werner Kühlbrandt

    (Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany)

Abstract

Transport proteins: sodium-free protein exchange Transport of solutes across biological membranes is carried out by specialized secondary transport proteins in the lipid bilayer. In this paper, the authors report the structures of the sodium-independent membrane antiporter CaiT isolated from two microorganisms, Escherichia coli and Proteus mirabilis. CaiT catalyses transmembrane exchange of L-carnitine and γ-butyrobetaine. The three-dimensional architecture of CaiT is found to resemble that of the Na+-dependent transporters LeuT and BetP — but in CaiT, a methionine sulphur takes the place and serves the same function as the sodium ion.

Suggested Citation

  • Sabrina Schulze & Stefan Köster & Ulrike Geldmacher & Anke C. Terwisscha van Scheltinga & Werner Kühlbrandt, 2010. "Structural basis of Na+-independent and cooperative substrate/product antiport in CaiT," Nature, Nature, vol. 467(7312), pages 233-236, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7312:d:10.1038_nature09310
    DOI: 10.1038/nature09310
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    Cited by:

    1. Heidi Koldsø & Pernille Noer & Julie Grouleff & Henriette Elisabeth Autzen & Steffen Sinning & Birgit Schiøtt, 2011. "Unbiased Simulations Reveal the Inward-Facing Conformation of the Human Serotonin Transporter and Na+ Ion Release," PLOS Computational Biology, Public Library of Science, vol. 7(10), pages 1-14, October.

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