8IP3

Cryo-EM structure of hMRS2-Mg

8IP3 の概要

• エントリーDOI: 10.2210/pdb8ip3/pdb
• EMDBエントリー: 35630
• 分子名称: Magnesium transporter MRS2 homolog, mitochondrial, CHLORIDE ION, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: pentamer, metal transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 257985.47

構造登録者

Li, M.,Li, Y.,Yang, X.,Shen, Y.Q. (登録日: 2023-03-14, 公開日: 2023-06-14, 最終更新日: 2023-08-30)

主引用文献

Li, M.,Li, Y.,Lu, Y.,Li, J.,Lu, X.,Ren, Y.,Wen, T.,Wang, Y.,Chang, S.,Zhang, X.,Yang, X.,Shen, Y.
Molecular basis of Mg 2+ permeation through the human mitochondrial Mrs2 channel.
Nat Commun, 14:4713-4713, 2023

PubMed Abstract: 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.

PubMed: 37543649
DOI: 10.1038/s41467-023-40516-2

実験手法

ELECTRON MICROSCOPY (2.6 Å)