Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	P-type ATPase magnesium transporter MgtA acts as a dimer.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 32, Issue 9, Page 1633-1643, Year 2025
Publish date	Jun 23, 2025
Authors	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 /
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 ...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.
External links	Nat Struct Mol Biol / PubMed:40550995 / PubMed Central
Methods	EM (single particle)
Resolution	2.93 - 3.87 Å
Structure data	42794 8uy7 EMDB-42794, PDB-8uy7: Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 Method: EM (single particle) / Resolution: 2.93 Å 42795 8uy8 EMDB-42795, PDB-8uy8: Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 in C1 Method: EM (single particle) / Resolution: 3.03 Å 42796 8uy9 EMDB-42796, PDB-8uy9: Magnesium transporter MgtA monomer from E. coli in 5 mM MgCl2 Method: EM (single particle) / Resolution: 3.65 Å 42797 8uya EMDB-42797, PDB-8uya: Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 and 5 mM ATP Method: EM (single particle) / Resolution: 3.72 Å 42798 8uyb EMDB-42798, PDB-8uyb: Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 and 5 mM ATPyS Method: EM (single particle) / Resolution: 3.87 Å 42799 8uyc EMDB-42799, PDB-8uyc: Magnesium transporter MgtA dimer from E. coli in 5 mM MgCl2 and 5 mM ADP Method: EM (single particle) / Resolution: 3.75 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM
Source	escherichia coli (E. coli) escherichia coli k-12 (bacteria)
Keywords	MEMBRANE PROTEIN / magnesium / transport / dimer / oligomer / cryo-EM / P-type ATPase / ion translocation