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TitleStructure of the Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 49, Page 31166-31176, Year 2020
Publish dateDec 8, 2020
AuthorsBin Li / Kaiduan Zhang / Yong Nie / Xianping Wang / Yan Zhao / Xuejun C Zhang / Xiao-Lei Wu /
PubMed AbstractMultiple 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 ...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 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.
External linksProc Natl Acad Sci U S A / PubMed:33229520 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

30567

7d3u

EMDB-30567, PDB-7d3u:
Structure of Mrp complex from Dietzia sp. DQ12-45-1b
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

Source
  • dietzia sp. dq12-45-1b (bacteria)
KeywordsMEMBRANE PROTEIN / Sodium/proton antiporter

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