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-Structure paper
| タイトル | P-type ATPase magnesium transporter MgtA acts as a dimer. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 32, Issue 9, Page 1633-1643, Year 2025 |
| 掲載日 | 2025年6月23日 |
著者 | 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 要旨 | 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. |
リンク | Nat Struct Mol Biol / PubMed:40550995 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.93 - 3.87 Å |
| 構造データ | EMDB-42794, PDB-8uy7: EMDB-42795, PDB-8uy8: EMDB-42796, PDB-8uy9: EMDB-42797, PDB-8uya: EMDB-42798, PDB-8uyb: EMDB-42799, PDB-8uyc: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-HOH: ![]() ChemComp-ATP: ![]() ChemComp-AGS: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / magnesium / transport / dimer / oligomer / cryo-EM / P-type ATPase / ion translocation |
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