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<p>Magnesium (Mg<sup>2+</sup>) uptake systems are present in all domains of life, consistent with the vital role of this ion. P-type ATPase Mg<sup>2+</sup> importers are required for bacterial growth when Mg<sup>2+</sup> is limiting or during pathogenesis. However, insights into their mechanisms of action are missing. Here we solved the cryo-EM structure of the Mg<sup>2+</sup> transporter MgtA from <i>Escherichia coli</i>. 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<sup>2+</sup>, 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.</p>

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P-type ATPase magnesium transporter MgtA acts as a dimer

  • 期刊论文

  • 发表日期：

    2025年6月23日

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  • Rilee Zeinert,
  • Fei Zhou,
  • Pedro Franco,
  • Jonathan Zöller,
  • Zaid K. Madni,
  • Henry Lessen,
  • L. Aravind,
  • Julian D. Langer,
  • Alexander J. Sodt,
  • Gisela Storz,
  • Doreen Matthies

摘要

Magnesium (Mg2+) uptake systems are present in all domains of life, consistent with the vital role of this ion. P-type ATPase Mg2+ importers are required for bacterial growth when Mg2+ is limiting or during pathogenesis. However, insights into their mechanisms of action are missing. Here we solved the cryo-EM structure of the Mg2+ 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 Mg2+, 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.