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

Sabrina Schulze, Stefan Köster, Ulrike Geldmacher, Anke C. Terwisscha van Scheltinga and Werner Kühlbrandt ()
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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
Werner Kühlbrandt: Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438 Frankfurt am Main, Germany

Nature, 2010, vol. 467, issue 7312, 233-236

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.

Date: 2010
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DOI: 10.1038/nature09310

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