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-Structure paper
タイトル | Molecular basis of Mg permeation through the human mitochondrial Mrs2 channel. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 4713, Year 2023 |
掲載日 | 2023年8月5日 |
著者 | Ming Li / Yang Li / Yue Lu / Jianhui Li / Xuhang Lu / Yue Ren / Tianlei Wen / Yaojie Wang / Shenghai Chang / Xing Zhang / Xue Yang / Yuequan Shen / |
PubMed 要旨 | Mitochondrial RNA splicing 2 (Mrs2), a eukaryotic CorA ortholog, enables Mg to permeate the inner mitochondrial membrane and plays an important role in mitochondrial metabolic function. However, the ...Mitochondrial RNA splicing 2 (Mrs2), a eukaryotic CorA ortholog, enables Mg to permeate the inner mitochondrial membrane and plays an important role in mitochondrial metabolic function. However, the mechanism by which Mrs2 permeates Mg 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 Mg uptake assays show that the R-ring may function as a charge repulsion barrier, and Cl may function as a ferry to jointly gate Mg permeation in hMrs2. In addition, the membrane potential is likely to be the driving force for Mg permeation. Our results provide insights into the channel assembly and Mg permeation of hMrs2. |
リンク | Nat Commun / PubMed:37543649 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.5 - 2.9 Å |
構造データ | EMDB-35630, PDB-8ip3: EMDB-35631, PDB-8ip4: EMDB-35632, PDB-8ip5: EMDB-35633, PDB-8ip6: |
化合物 | ChemComp-CL: ChemComp-MG: ChemComp-HOH: |
由来 |
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キーワード | METAL TRANSPORT / pentamer |