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Showing 1–4 of 4 results
Advanced filters: Author: Anke C. Terwisscha van Scheltinga Clear advanced filters

  • Transport of solutes across biological membranes is carried out by specialized secondary transport proteins in the lipid bilayer. These authors report structures of the sodium-independent carnitine/butyrobetaine antiporter CaiT from two microorganisms. The three-dimensional architecture of CaiT resembles that of the Na+-dependent transporters LeuT and BetP, but in CaiT a methionine sulphur takes the place of the Na+ ion to coordinate the substrate in the central transport site, enabling Na+-independent transport to occur.

    • Sabrina Schulze
    • Stefan Köster
    • Werner Kühlbrandt
    Research
    Nature
    Volume: 467, P: 233-236

  • This paper presents the first X-ray structure of a member of the the betaine/choline/carnitine transporter family. This Na+-coupled symporter (BetP) has the same overall fold as other unrelated Na+-coupled transporters and is captured in an intermediate conformation, whereby the substrate (glycine betaine) is occluded from both sides of the membrane.

    • Susanne Ressl
    • Anke C. Terwisscha van Scheltinga
    • Christine Ziegler
    Research
    Nature
    Volume: 458, P: 47-52