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	Distinct transport cycle and lipid regulation of a Mg2+-transporting P-type ATPase, MgtA.
Journal, issue, pages	Res Sq, Year 2026
Publish date	May 4, 2026
Authors	Howard Young / Muhammad Bashir Khan / Joseph Primeau / Paramita Chaudhuri-Basu / Lucie Bergdoll / Ludovic Renault / J Preben Morth / M Joanne Lemieux
PubMed Abstract	P-type ATPases represent an evolutionarily conserved superfamily of ion, lipid, and peptide pumps found across all domains of life. Among the substrates transported by P-type ATPases, Mg2+ is of ...P-type ATPases represent an evolutionarily conserved superfamily of ion, lipid, and peptide pumps found across all domains of life. Among the substrates transported by P-type ATPases, Mg2+ is of critical importance in bacterial, fungal, and plant cellular homeostasis. A bacterial P-type ATPase found in Gram-negative bacteria, Mg2+ transporter A (MgtA), facilitates the transport of Mg2+ from the periplasm to the cytoplasm under conditions of Mg2+ starvation. MgtA is a cardiolipin-sensitive integral membrane ion-transporter that scavenges Mg2+ during bacterial infection and pathogenesis. Here, we determined cryo-EM structures of MgtA capturing three distinct states along the Mg2+ transport cycle, including a phosphorylated E2-P intermediate (2.6 Å resolution), an E1-like conformation stabilized by the peptide regulator MgtR (2.7 Å resolution), and an E1-like ATP-bound state (2.8 Å resolution). These three conformations reveal the binding of Mg2+ in the transmembrane domain coordinated in a novel site involving Ser702 and Asn706 on M5, Ser773 and Asp777 on M7, and Ser821 and Thr824 on M8. In the E2-P conformation, the phosphate analog BeF3 is bound in close proximity to the catalytic aspartate, Asp361, suggesting that it represents a covalent aspartylphosphate intermediate. In the presence of AMPPCP, Mg2+ remains bound in the transmembrane domain and the ATP analog is bound in a catalytically competent conformation. Overall, the structures reveal distinct steps in the transport cycle of MgtA compared to other P-type ATPases, as well as lipid binding sites that fill gaps in our understanding of transport regulation.
External links	Res Sq / PubMed:42147146 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.59 - 3.55 Å
Structure data	45025 9byb EMDB-45025, PDB-9byb: Cryo-EM structure of the magnesium transporter MgtA in the E2 conformation with bound lipids and Mg2+ Method: EM (single particle) / Resolution: 3.29 Å 48191 9me9 EMDB-48191, PDB-9me9: Cryo-EM structure of the magnesium transporter MgtA in an E1-like conformation with bound Mg2+ ions Method: EM (single particle) / Resolution: 3.2 Å 48534 9mqm EMDB-48534, PDB-9mqm: Cryo-EM of MgtA in the E2-P state with bound Mg2+ at 3.1 angstrom resolution Method: EM (single particle) / Resolution: 3.07 Å 48602 9mt7 EMDB-48602, PDB-9mt7: Cryo-EM Structure of the Magnesium Transporter MgtA in the E2 Conformation Bound to Mg2+ Method: EM (single particle) / Resolution: 3.23 Å 48855 9n3v EMDB-48855, PDB-9n3v: Cryo-EM structure of the magnesium transporter MgtA in E1-like and E2-P conformations at 2.59 angstroms Method: EM (single particle) / Resolution: 2.65 Å 48923 9n5j EMDB-48923, PDB-9n5j: Cryo-EM structure of the magnesium transporter MgtA in the E2 conformation with bound beryllium fluoride (BeF3-) and Mg2+ at 2.65 A resolution. Method: EM (single particle) / Resolution: 2.59 Å 49450 9nhz EMDB-49450, PDB-9nhz: Cryo-EM structure of an MgtA tetramer in E2-P and E1-like states Method: EM (single particle) / Resolution: 2.73 Å 72125 9q1e EMDB-72125, PDB-9q1e: Cryo-EM Structure of the MgtA Tetramer at 2.7 A Resolution Method: EM (single particle) / Resolution: 2.69 Å 72280 9q6o EMDB-72280, PDB-9q6o: Cryo-EM Structure of MgtA in the E2-P State at 2.7 A Resolution Method: EM (single particle) / Resolution: 2.65 Å 74405 9zlk EMDB-74405, PDB-9zlk: Cryo-EM structure of MgtA with bound AMPPCP and magnesium Method: EM (single particle) / Resolution: 2.79 Å PDB-9ejn: Crystal structure of magnesium-transporting ATPase MgtA in an E1-like magnesium-bound state Method: X-RAY DIFFRACTION / Resolution: 3.55 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-CDL: CARDIOLIPIN / phospholipidYM ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-LMT: DODECYL-BETA-D-MALTOSIDE / detergentYM ChemComp-HOH: WATER ChemComp-ACP: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogueYM ChemComp-K*: Unknown entry
Source	lactococcus lactis subsp. lactis cv56 (lactic acid bacteria) lactococcus lactis subsp. lactis (lactic acid bacteria) lactococcus cremoris (lactic acid bacteria)
Keywords	METAL TRANSPORT / P-type ATPase / Membrane protein / Magnesium Ion / TRANSPORT PROTEIN / membrane Transport / MgtA / AMPPCP