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Specialized transport proteins in the lipid bilayer perform the translocation of solutes across biological membranes. The prokaryotic Lcarnitine/?butyrobetaine transporter CaiT is a member of the betaine/carnitine/choline transporter (BCCT) family. However, CaiT is an interesting exception within the BCCT family since the transporter functions as a Na+ and H+ independent antiporter, while most members of the BCCT family require either an additional sodium ion or a proton to transport substrates into the cell. The threedimensional Xray crystal structure of CaiT reveals two different substratebinding sites within the protein and provides insights into important residues that directly interact with the two substrates Lcarnitine and ?butyrobetaine and enable substrate binding and transport without the need of an additional cation. The comparison of two threedimension CaiT structures in two different states together with results obtained from functional studies allowed the formulation of a model for the allosterically regulated substrate/product antiport mechanism in CaiT, which is also very likely conserved in eukaryotic Lcarnitine transporters.
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