National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
ZIA HD008998
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
ZIA HD008855
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
ZIA HD008955
米国
National Institutes of Health/National Library of Medicine (NIH/NLM)
LM594244
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1FI2GM146628-01
米国
German Research Foundation (DFG)
3542/1-1
ドイツ
引用
ジャーナル: Nat Struct Mol Biol / 年: 2025 タイトル: P-type ATPase magnesium transporter MgtA acts as a dimer. 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 / 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.
超分子 #1: Magnesium transporter MgtA from Escherichia coli in the dimeric f...
超分子
名称: Magnesium transporter MgtA from Escherichia coli in the dimeric form in the presence of 5 mM MgCl2 and 5 mM ATP タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1
フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 撮影したグリッド数: 1 / 実像数: 14585 / 平均露光時間: 3.995 sec. / 平均電子線量: 50.0 e/Å2 詳細: A dataset was collected with a dose rate of 9 A/px/s (~7.5 on the camera through the sample), exposure time 0.0665 s/frame (~0.833 e-/A2) and total exposure time of 3.995 s per movie (~50 e- ...詳細: A dataset was collected with a dose rate of 9 A/px/s (~7.5 on the camera through the sample), exposure time 0.0665 s/frame (~0.833 e-/A2) and total exposure time of 3.995 s per movie (~50 e-/A2), resulting in a total of 14,585 movies with 60 frames each.