Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump.

Abstract:

: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 three-dimensional structure of the Mrp complex from a Dietzia sp. strain solved at 3.0-Å 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.

authors

Li B,Zhang K,Nie Y,Wang X,Zhao Y,Zhang XC,Wu XL

doi

10.1073/pnas.2006276117

subject

Has Abstract

pub_date

2020-12-08 00:00:00

pages

31166-31176

issue

49

eissn

0027-8424

issn

1091-6490

pii

2006276117

journal_volume

117

pub_type

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