8UYC

Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 and 5 mM ADP

8UYC の概要

• エントリーDOI: 10.2210/pdb8uyc/pdb
• EMDBエントリー: 42794 42795 42796 42797 42798 42799
• 分子名称: Magnesium-transporting ATPase, P-type 1, MAGNESIUM ION (2 entities in total)
• 機能のキーワード: magnesium, transport, membrane protein, dimer, oligomer, cryo-em, p-type atpase, ion translocation
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 200931.95

構造登録者

Zeinert, R.,Zhou, F.,Cavalcanti Franco, P.H.,Zoeller, J.,Lessen, H.,Iyer, A.,Langer, J.D.,Sodt, A.J.,Storz, G.,Matthies, D. (登録日: 2023-11-13, 公開日: 2024-11-27, 最終更新日: 2025-10-01)

主引用文献

Zeinert, R.,Zhou, F.,Franco, P.,Zoller, J.,Madni, Z.K.,Lessen, H.,Aravind, L.,Langer, J.D.,Sodt, A.J.,Storz, G.,Matthies, D.
P-type ATPase magnesium transporter MgtA acts as a dimer.
Nat.Struct.Mol.Biol., 32:1633-1643, 2025

PubMed Abstract: Magnesium (Mg) uptake systems are present in all domains of life, consistent with the vital role of this ion. P-type ATPase Mg importers are required for bacterial growth when Mg is limiting or during pathogenesis. However, insights into their mechanisms of action are missing. Here we solved the cryo-EM structure of the Mg transporter MgtA from Escherichia coli. We obtained high-resolution structures of both homodimeric (2.9 Å) and monomeric (3.6 Å) forms. The dimer structure is formed by multiple contacts between residues in adjacent soluble N and P subdomains. Our structures revealed an ion, assigned as Mg, in the transmembrane segment. Moreover, we detected two cytoplasmic ion-binding sites and determined the structure of the N-terminal tail. Sequence conservation, mutagenesis and ATPase assays indicate dimerization, the ion-binding sites and the N-terminal tail facilitate cation transport or serve regulatory roles.

PubMed: 40550995
DOI: 10.1038/s41594-025-01593-7

実験手法

ELECTRON MICROSCOPY (3.75 Å)