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Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations

Author

Listed:
  • Yongchan Lee

    (Max Planck Institute of Biophysics
    Yokohama City University)

  • Outi Haapanen

    (University of Helsinki)

  • Anton Altmeyer

    (Goethe University
    Goethe University)

  • Werner Kühlbrandt

    (Max Planck Institute of Biophysics)

  • Vivek Sharma

    (University of Helsinki
    University of Helsinki)

  • Volker Zickermann

    (Goethe University
    Goethe University)

Abstract

Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are closely related to the membrane domain of respiratory complex I. We determined the structure of the Mrp antiporter from Bacillus pseudofirmus by electron cryo-microscopy at 2.2 Å resolution. The structure resolves more than 99% of the sidechains of the seven membrane subunits MrpA to MrpG plus 360 water molecules, including ~70 in putative ion translocation pathways. Molecular dynamics simulations based on the high-resolution structure revealed details of the antiport mechanism. We find that switching the position of a histidine residue between three hydrated pathways in the MrpA subunit is critical for proton transfer that drives gated trans-membrane sodium translocation. Several lines of evidence indicate that the same histidine-switch mechanism operates in respiratory complex I.

Suggested Citation

  • Yongchan Lee & Outi Haapanen & Anton Altmeyer & Werner Kühlbrandt & Vivek Sharma & Volker Zickermann, 2022. "Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33640-y
    DOI: 10.1038/s41467-022-33640-y
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    References listed on IDEAS

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    1. Hongjun Yu & Dominik K. Haja & Gerrit J. Schut & Chang-Hao Wu & Xing Meng & Gongpu Zhao & Huilin Li & Michael W. W. Adams, 2020. "Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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    Cited by:

    1. Adel Beghiah & Patricia Saura & Sofia Badolato & Hyunho Kim & Johanna Zipf & Dirk Auman & Ana P. Gamiz-Hernandez & Johan Berg & Grant Kemp & Ville R. I. Kaila, 2024. "Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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