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

@article{Schulze2010StructuralBO,
  title={Structural basis of Na+-independent and cooperative substrate/product antiport in CaiT},
  author={Sabrina Schulze and Stefan K{\"o}ster and Ulrike Geldmacher and Anke C. Terwisscha van Scheltinga and Werner K{\"u}hlbrandt},
  journal={Nature},
  year={2010},
  volume={467},
  pages={233-236}
}
Transport of solutes across biological membranes is performed by specialized secondary transport proteins in the lipid bilayer, and is essential for life. Here we report the structures of the sodium-independent carnitine/butyrobetaine antiporter CaiT from Proteus mirabilis (PmCaiT) at 2.3-Å and from Escherichia coli (EcCaiT) at 3.5-Å resolution. CaiT belongs to the family of betaine/carnitine/choline transporters (BCCT), which are mostly Na+ or H+ dependent, whereas EcCaiT is Na+ and H… 
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