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Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP

Author

Listed:
  • Camilo Perez

    (Max-Planck Institute of Biophysics)

  • Caroline Koshy

    (Max-Planck Institute of Biophysics)

  • Özkan Yildiz

    (Max-Planck Institute of Biophysics)

  • Christine Ziegler

    (Max-Planck Institute of Biophysics
    Institute of Biophysics and Biophysical Chemistry, University of Regensburg, D-93053 Regensburg, Germany)

Abstract

The crystal structure of the osmotically regulated symporter BetP is reported in four new conformations, providing information about the key conformational changes that take place during the transport cycle.

Suggested Citation

  • Camilo Perez & Caroline Koshy & Özkan Yildiz & Christine Ziegler, 2012. "Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP," Nature, Nature, vol. 490(7418), pages 126-130, October.
    • Handle: RePEc:nat:nature:v:490:y:2012:i:7418:d:10.1038_nature11403
    DOI: 10.1038/nature11403
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    Cited by:

    1. Wenhao Cui & Yange Niu & Zejian Sun & Rui Liu & Lei Chen, 2023. "Structures of human SGLT in the occluded state reveal conformational changes during sugar transport," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Hyun Deok Song & Fangqiang Zhu, 2015. "Conformational Changes in Two Inter-Helical Loops of Mhp1 Membrane Transporter," PLOS ONE, Public Library of Science, vol. 10(7), pages 1-19, July.

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