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

Yongchan Lee, Outi Haapanen, Anton Altmeyer, Werner Kühlbrandt, Vivek Sharma () and Volker Zickermann ()
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Yongchan Lee: Max Planck Institute of Biophysics
Outi Haapanen: University of Helsinki
Anton Altmeyer: Goethe University
Werner Kühlbrandt: Max Planck Institute of Biophysics
Vivek Sharma: University of Helsinki
Volker Zickermann: Goethe University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-33640-y

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