Magnesium Transporter MgtA revealed as a Dimeric P-type ATPase.

ABSTRACT: Magnesium (Mg²⁺) uptake systems are present in all domains of life given the vital role of this ion. Bacteria acquire Mg²⁺ via conserved Mg²⁺ channels and transporters. The transporters are required for growth when Mg²⁺ is limiting or during bacterial pathogenesis, but, despite their significance, there are no known structures for these transporters. Here we report the first structure of the Mg²⁺ transporter MgtA solved by single particle cryo-electron microscopy (cryo-EM). Using mild membrane extraction, we obtained high resolution structures of both a homodimeric form (2.9 Å), the first for a P-type ATPase, and a monomeric form (3.6 Å). Each monomer unit of MgtA displays a structural architecture that is similar to other P-type ATPas

SUBMITTER: Zeinert R 

PROVIDER: S-EPMC10925321 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature