Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter.

ABSTRACT: 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 Anoxybacillus flavithermus 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 tr

SUBMITTER: Steiner J 

PROVIDER: S-EPMC7419157 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature