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Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH

Author

Listed:
  • Carola Hunte

    (Max Planck Institute of Biophysics)

  • Emanuela Screpanti

    (Max Planck Institute of Biophysics)

  • Miro Venturi

    (Max Planck Institute of Biophysics)

  • Abraham Rimon

    (Hebrew University of Jerusalem)

  • Etana Padan

    (Hebrew University of Jerusalem)

  • Hartmut Michel

    (Max Planck Institute of Biophysics)

Abstract

The control by Na+/H+ antiporters of sodium/proton concentration and cell volume is crucial for the viability of all cells. Adaptation to high salinity and/or extreme pH in plants and bacteria or in human heart muscles requires the action of Na+/H+ antiporters. Their activity is tightly controlled by pH. Here we present the crystal structure of pH-downregulated NhaA, the main antiporter of Escherichia coli and many enterobacteria. A negatively charged ion funnel opens to the cytoplasm and ends in the middle of the membrane at the putative ion-binding site. There, a unique assembly of two pairs of short helices connected by crossed, extended chains creates a balanced electrostatic environment. We propose that the binding of charged substrates causes an electric imbalance, inducing movements, that permit a rapid alternating-access mechanism. This ion-exchange machinery is regulated by a conformational change elicited by a pH signal perceived at the entry to the cytoplasmic funnel.

Suggested Citation

  • Carola Hunte & Emanuela Screpanti & Miro Venturi & Abraham Rimon & Etana Padan & Hartmut Michel, 2005. "Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH," Nature, Nature, vol. 435(7046), pages 1197-1202, June.
    • Handle: RePEc:nat:nature:v:435:y:2005:i:7046:d:10.1038_nature03692
    DOI: 10.1038/nature03692
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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. 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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