期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 117, 期 49, 页码 31166-31176出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2006276117
关键词
Na plus /H plus antiporter; Mrp complex; cryo-EM; complex I; energy coupling
资金
- National Key R&D Program of China [2018YFA0902100, 2018YFA0902103]
- Chinese Academy of Sciences Strategic Priority Research Program [XDB08020301, XDB37030304, XDB37030301]
- National Natural Science Foundation of China [31770120, 31971134]
Multiple resistance and pH adaptation (Mrp) complexes are sophisticated cation/proton exchangers found in a vast variety of alkaliphilic and/or halophilic microorganisms, and are critical for their survival in highly challenging environments. This family of antiporters is likely to represent the ancestor of cation pumps found in many redox-driven transporter complexes, including the complex I of the respiratory chain. Here, we present the threedimensional structure of the Mrp complex from a Dietzia sp. strain solved at 3.0-angstrom resolution using the single-particle cryoelectron microscopy method. Our structure-based mutagenesis and functional analyses suggest that the substrate translocation pathways for the driving substance protons and the substrate sodium ions are separated in two modules and that symmetry-restrained conformational change underlies the functional cycle of the transporter. Our findings shed light on mechanisms of redox-driven primary active transporters, and explain how driving substances of different electric charges may drive similar transport processes.
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