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A two-domain elevator mechanism for sodium/proton antiport

Author

Listed:
  • Chiara Lee

    (Imperial College London, London SW7 2AZ, UK)

  • Hae Joo Kang

    (Imperial College London, London SW7 2AZ, UK)

  • Christoph von Ballmoos

    (Centre for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden)

  • Simon Newstead

    (Imperial College London, London SW7 2AZ, UK
    Present address: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.)

  • Povilas Uzdavinys

    (Centre for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden)

  • David L. Dotson

    (Center for Biological Physics, Arizona State University)

  • So Iwata

    (Imperial College London, London SW7 2AZ, UK
    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Chilton, Oxfordshire OX11 0DE, UK
    Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell, Oxford, Didcot, Oxfordshire OX11 0FA, UK)

  • Oliver Beckstein

    (Center for Biological Physics, Arizona State University)

  • Alexander D. Cameron

    (Imperial College London, London SW7 2AZ, UK
    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Chilton, Oxfordshire OX11 0DE, UK
    Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell, Oxford, Didcot, Oxfordshire OX11 0FA, UK
    School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK)

  • David Drew

    (Imperial College London, London SW7 2AZ, UK
    Centre for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden)

Abstract

The X-ray crystal structure of NapA, a Na+/H+ antiporter from Thermus thermophilus, in an active, outward-facing state is reported; comparisons to the structure of a related transporter in a low pH/inactivated, inward-facing state show the conformational changes that occur when the membrane protein moves from an inward-facing to an outward-facing state, suggesting that Na+/H+ antiporters operate by a two-domain rocking bundle model.

Suggested Citation

  • Chiara Lee & Hae Joo Kang & Christoph von Ballmoos & Simon Newstead & Povilas Uzdavinys & David L. Dotson & So Iwata & Oliver Beckstein & Alexander D. Cameron & David Drew, 2013. "A two-domain elevator mechanism for sodium/proton antiport," Nature, Nature, vol. 501(7468), pages 573-577, September.
    • Handle: RePEc:nat:nature:v:501:y:2013:i:7468:d:10.1038_nature12484
    DOI: 10.1038/nature12484
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    Cited by:

    1. Iven Winkelmann & Povilas Uzdavinys & Ian M. Kenney & Joseph Brock & Pascal F. Meier & Lina-Marie Wagner & Florian Gabriel & Sukkyeong Jung & Rei Matsuoka & Christoph Ballmoos & Oliver Beckstein & Dav, 2022. "Crystal structure of the Na+/H+ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Yuhang Wang & Chengcai Pan & Qihao Chen & Qing Xie & Yiwei Gao & Lingli He & Yue Li & Yanli Dong & Xingyu Jiang & Yan Zhao, 2023. "Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Atsushi Yamagata & Yoshiko Murata & Kosuke Namba & Tohru Terada & Shuya Fukai & Mikako Shirouzu, 2022. "Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Ashutosh Gulati & Surabhi Kokane & Annemarie Perez-Boerema & Claudia Alleva & Pascal F. Meier & Rei Matsuoka & David Drew, 2024. "Structure and mechanism of the K+/H+ exchanger KefC," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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