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Molecular basis of transport and regulation in the Na+/betaine symporter BetP

Author

Listed:
  • Susanne Ressl

    (Max Planck Institute of Biophysics)

  • Anke C. Terwisscha van Scheltinga

    (Max Planck Institute of Biophysics)

  • Clemens Vonrhein

    (Global Phasing Ltd, Sheraton House, Castle Park, Cambridge CB3 0AX, UK)

  • Vera Ott

    (Institut für Biochemie, Universität zu Köln)

  • Christine Ziegler

    (Max Planck Institute of Biophysics)

Abstract

Osmoregulated transporters sense intracellular osmotic pressure and respond to hyperosmotic stress by accumulation of osmolytes to restore normal hydration levels. Here we report the determination of the X-ray structure of a member of the family of betaine/choline/carnitine transporters, the Na+-coupled symporter BetP from Corynebacterium glutamicum, which is a highly effective osmoregulated uptake system for glycine betaine. Glycine betaine is bound in a tryptophan box occluded from both sides of the membrane with aromatic side chains lining the transport pathway. BetP has the same overall fold as three unrelated Na+-coupled symporters. Whereas these are crystallized in either the outward-facing or the inward-facing conformation, the BetP structure reveals a unique intermediate conformation in the Na+-coupled transport cycle. The trimeric architecture of BetP and the break in three-fold symmetry by the osmosensing C-terminal helices suggest a regulatory mechanism of Na+-coupled osmolyte transport to counteract osmotic stress.

Suggested Citation

  • Susanne Ressl & Anke C. Terwisscha van Scheltinga & Clemens Vonrhein & Vera Ott & Christine Ziegler, 2009. "Molecular basis of transport and regulation in the Na+/betaine symporter BetP," Nature, Nature, vol. 458(7234), pages 47-52, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7234:d:10.1038_nature07819
    DOI: 10.1038/nature07819
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