P-type ATPase magnesium transporter MgtA acts as a dimer.

ABSTRACT: 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

SUBMITTER: Zeinert R 

PROVIDER: S-EPMC12684380 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature