EMD-35632

Single-particle
2.5 Å
EMD-35632 Deposition: 14/03/2023
Map released: 14/06/2023
Last modified: 30/08/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-35632

Cryo-EM structure of hMRS2-lowEDTA

EMD-35632

Single-particle
2.5 Å
EMD-35632 Deposition: 14/03/2023
Map released: 14/06/2023
Last modified: 30/08/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: human MRS2
Fitted models: 8ip5 (Avg. Q-score: 0.563)

Deposition Authors: Li M , Li Y , Yang X , Shen YQ
Molecular basis of Mg 2+ permeation through the human mitochondrial Mrs2 channel.
Li M , Li Y , Lu Y , Li J , Lu X , Ren Y , Wen T , Wang Y , Chang S, Zhang X , Yang X , Shen Y
(2023) Nat Commun , 14 , 4713 - 4713
PUBMED: 37543649
DOI: doi:10.1038/s41467-023-40516-2
ISSN: 2041-1723
Abstract:
Mitochondrial RNA splicing 2 (Mrs2), a eukaryotic CorA ortholog, enables Mg2+ to permeate the inner mitochondrial membrane and plays an important role in mitochondrial metabolic function. However, the mechanism by which Mrs2 permeates Mg2+ remains unclear. Here, we report four cryo-electron microscopy (cryo-EM) reconstructions of Homo sapiens Mrs2 (hMrs2) under various conditions. All of these hMrs2 structures form symmetrical pentamers with very similar pentamer and protomer conformations. A special structural feature of Cl--bound R-ring, which consists of five Arg332 residues, was found in the hMrs2 structure. Molecular dynamics simulations and mitochondrial Mg2+ uptake assays show that the R-ring may function as a charge repulsion barrier, and Cl- may function as a ferry to jointly gate Mg2+ permeation in hMrs2. In addition, the membrane potential is likely to be the driving force for Mg2+ permeation. Our results provide insights into the channel assembly and Mg2+ permeation of hMrs2.