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TitleStructure and mechanism of the Mrp complex, an ancient cation/proton antiporter.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJul 31, 2020
AuthorsJulia Steiner / Leonid Sazanov /
PubMed AbstractMultiple resistance and pH adaptation (Mrp) antiporters are multi-subunit Na (or K)/H exchangers representing an ancestor of many essential redox-driven proton pumps, such as respiratory complex I. ...Multiple resistance and pH adaptation (Mrp) antiporters are multi-subunit Na (or K)/H exchangers representing an ancestor of many essential redox-driven proton pumps, such as respiratory complex I. The mechanism of coupling between ion or electron transfer and proton translocation in this large protein family is unknown. Here, we present the structure of the Mrp complex from solved by cryo-EM at 3.0 Å resolution. It is a dimer of seven-subunit protomers with 50 trans-membrane helices each. Surface charge distribution within each monomer is remarkably asymmetric, revealing probable proton and sodium translocation pathways. On the basis of the structure we propose a mechanism where the coupling between sodium and proton translocation is facilitated by a series of electrostatic interactions between a cation and key charged residues. This mechanism is likely to be applicable to the entire family of redox proton pumps, where electron transfer to substrates replaces cation movements.
External linksElife / PubMed:32735215 / PubMed Central
MethodsEM (single particle)
Resolution2.98 Å
Structure data

11027

6z16

EMDB-11027, PDB-6z16:
Structure of the Mrp antiporter complex
Method: EM (single particle) / Resolution: 2.98 Å

Chemicals

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-K:
Unknown entry

Source
  • Anoxybacillus flavithermus WK1 (bacteria)
  • anoxybacillus flavithermus (strain dsm 21510 / wk1) (bacteria)
KeywordsMEMBRANE PROTEIN / Mrp antiporter / sodium/proton exchanger / bioenergetics / complex

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