Lee 2022 Nat Commun: Difference between revisions
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Latest revision as of 15:58, 22 March 2023
Lee Y, Haapanen O, Altmeyer A, KΓΌhlbrandt W, Sharma V, Zickermann V (2022) Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations. https://doi.org/10.1038/s41467-022-33640-y |
Β» Nat Commun 13:6091. PMID: 36241630 Open Access
Lee Yongchan, Haapanen Outi, Altmeyer Anton, Kuehlbrandt Werner, Sharma Vivek, Zickermann Volker (2022) Nat Commun
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 Γ 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.
β’ Bioblast editor: Plangger M
Labels: MiParea: mt-Structure;fission;fusion
Enzyme: Complex I