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TitleIon transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6091, Year 2022
Publish dateOct 14, 2022
AuthorsYongchan Lee / Outi Haapanen / Anton Altmeyer / Werner Kühlbrandt / Vivek Sharma / Volker Zickermann /
PubMed AbstractMultiple 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 ...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.
External linksNat Commun / PubMed:36241630 / PubMed Central
MethodsEM (single particle)
Resolution2.24 - 2.96 Å
Structure data

14124

7qru

EMDB-14124, PDB-7qru:
Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer
Method: EM (single particle) / Resolution: 2.24 Å

EMDB-15593: Structure of Bacillus pseudofirmus Mrp antiporter complex, dimer
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-15693: Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer, processed at original pixel size (0.837 A/pix)
Method: EM (single particle) / Resolution: 2.25 Å

Chemicals

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-HOH:
WATER / Water

Source
  • Alkalihalobacillus pseudofirmus (bacteria)
  • alkalihalophilus pseudofirmus (bacteria)
KeywordsMEMBRANE PROTEIN / Antiporter / Electron transport / Complex

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