ArticlePLoS biology2021
The structure of MgtE in the absence of magnesium provides new insights into channel gating.
Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Magnesium Transporters as Crucial Regulators of Bacterial Survival and Pathogenicity.Microorganisms · 2026Review
- Molecular bases of circadian magnesium rhythms across eukaryotes.FEBS letters · 2026Article
- Optimizing Magnesium Uptake in Lacticaseibacillus Rhamnosus To Advance Nutribiotic Strategies.Current microbiology · 2026Article
- Klebsiella pneumoniae employs a type VI secretion system to overcome microbiota-mediated colonization resistance.Nature communications · 2025Article
- The genesApplied and environmental microbiology · 2024Article
- Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms.Nature communications · 2023Article
- Novel MgActa biochimica et biophysica Sinica · 2023Article
- Ion selectivity mechanism of the MgtE channel for MgiScience · 2022Article
- Structural and functional comparison of magnesium transporters throughout evolution.Cellular and molecular life sciences : CMLS · 2022Review
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Authors and funding
23 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MgtE is a Mg2+ channel conserved in organisms ranging from prokaryotes to eukaryotes, including humans, and plays an important role in Mg2+ homeostasis. The previously determined MgtE structures in the Mg2+-bound, closed-state, and structure-based functional analyses of MgtE revealed that the binding of Mg2+ ions to the MgtE cytoplasmic domain induces channel inactivation to maintain Mg2+ homeostasis. There are no structures of the transmembrane (TM) domain for MgtE in Mg2+-free conditions, and the pore-opening mechanism has thus remained unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structure of the MgtE-Fab complex in the absence of Mg2+ ions. The Mg2+-free MgtE TM domain structure and its comparison with the Mg2+-bound, closed-state structure, together with functional analyses, showed the Mg2+-dependent pore opening of MgtE on the cytoplasmic side and revealed the kink motions of the TM2 and TM5 helices at the glycine residues, which are important for channel activity. Overall, our work provides structure-based mechanistic insights into the channel gating of MgtE.
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