ArticleNature communications2022
Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026Article
- Review
- Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.International journal of molecular sciences · 2026Article
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Proton Transfer through a Charged Conduit in Respiratory Complex I: Long-Range Effects and Conformational Gating.Journal of chemical information and modeling · 2025Article
- Nutrient Requirements Shape the Preferential Habitat of Allorhizobium vitis VAR03-1, a Commensal Bacterium, in the Rhizosphere of Arabidopsis thaliana.Plant & cell physiology · 2024Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- The polyextremophileApplied and environmental microbiology · 2024Article
- Role of Protonation States in the Stability of Molecular Dynamics Simulations of High-Resolution Membrane Protein Structures.The journal of physical chemistry. B · 2024Article
- Reversed oxidative TCA (roTCA) for carbon fixation by an Acidimicrobiia strain from a saline lake.The ISME journal · 2024Article
- Editorial: Computational and experimental insights in proton and ion translocating bioenergetic systems.Frontiers in chemistry · 2024Article
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- From the 'black box' to 'domino effect' mechanism: what have we learned from the structures of respiratory complex I.The Biochemical journal · 2023Review
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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