8UYB
Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 and 5 mM ATPyS
Summary for 8UYB
| Entry DOI | 10.2210/pdb8uyb/pdb |
| EMDB information | 42794 42795 42796 42797 42798 42799 |
| Descriptor | Magnesium-transporting ATPase, P-type 1, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total) |
| Functional Keywords | magnesium, transport, membrane protein, dimer, oligomer, cryo-em, p-type atpase, ion translocation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 201978.45 |
| Authors | Zeinert, R.,Zhou, F.,Cavalcanti Franco, P.H.,Zoeller, J.,Lessen, H.,Iyer, A.,Langer, J.D.,Sodt, A.J.,Storz, G.,Matthies, D. (deposition date: 2023-11-13, release date: 2024-11-27, Last modification date: 2025-07-09) |
| Primary citation | 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., 2025 Cited by 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: 40550995DOI: 10.1038/s41594-025-01593-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.87 Å) |
Structure validation
Download full validation report
