EMD-35631
Cryo-EM structure of hMRS-highEDTA
EMD-35631
Single-particle2.7 Å
![EMD-35631](https://www.ebi.ac.uk/emdb/images/entry/EMD-35631/400_35631.gif)
Map released: 14/06/2023
Last modified: 30/08/2023
Sample Organism:
Homo sapiens
Sample: human MRS2
Fitted models: 8ip4 (Avg. Q-score: 0.529)
Deposition Authors: Li M
,
Li Y
,
Yang X
,
Shen YQ
Sample: human MRS2
Fitted models: 8ip4 (Avg. Q-score: 0.529)
Deposition Authors: Li M
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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
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(2023) Nat Commun , 14 , 4713 - 4713
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.
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.