ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- How mutagenesis and laboratory conditions affect the genome of the metal-resistant bacteriumJournal of bacteriology · 2026Article
- Magnesium Transporters as Crucial Regulators of Bacterial Survival and Pathogenicity.Microorganisms · 2026Review
- Determinants of metal import and specificity in a bacterial transporter.bioRxiv : the preprint server for biology · 2026Article
- Conformational ensembles of the magnesium channel CorA reveal structural basis for channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A flow equilibrium model controlling cytoplasmic transition metal cation pools and preventing mis-metalation as exemplified for zinc homeostasis.Journal of bacteriology · 2025Review
- Rhodopsin from Haloquadratum walsbyi is a light-driven magnesium transporter.Nature communications · 2025Article
- Structure and function of the human mitochondrial MRS2 channel.Nature structural & molecular biology · 2025Article
- Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism.Nature structural & molecular biology · 2025Article
- MRS2 missense variation at Asp216 abrogates inhibitory MgProtein science : a publication of the Protein Society · 2024Article
- A flow equilibrium of zinc in cells ofJournal of bacteriology · 2024Article
- Mrs2-mediated mitochondrial magnesium uptake is essential for the regulation of MCU-mediated mitochondrial CaMitochondrion · 2024Article
- Could Life Have Started on Mars? Planetary Conditions That Assemble and Destroy Protocells.Life (Basel, Switzerland) · 2024Article
- Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms.Nature communications · 2023Article
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Conformation-specific Synthetic Antibodies Discriminate Multiple Functional States of the Ion Channel CorA.Journal of molecular biology · 2023Article
- Molecular basis of MgNature communications · 2023Article
- The human MRS2 magnesium-binding domain is a regulatory feedback switch for channel activity.Life science alliance · 2023Article
- Chloroplast magnesium transporters play essential but differential roles in maintaining magnesium homeostasis.Frontiers in plant science · 2023Article
- MgeLife · 2022Article
- Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family.eLife · 2022Article
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9 authors.
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Abstract
Despite the importance of Mg(2+) for numerous cellular activities, the mechanisms underlying its import and homeostasis are poorly understood. The CorA family is ubiquitous and is primarily responsible for Mg(2+) transport. However, the key questions-such as, the ion selectivity, the transport pathway, and the gating mechanism-have remained unanswered for this protein family. We present a 3.2 Å resolution structure of the archaeal CorA from Methanocaldococcus jannaschii, which is a unique complete structure of a CorA protein and reveals the organization of the selectivity filter, which is composed of the signature motif of this family. The structure reveals that polar residues facing the channel coordinate a partially hydrated Mg(2+) during the transport. Based on these findings, we propose a unique gating mechanism involving a helical turn upon the binding of Mg(2+) to the regulatory intracellular binding sites, and thus converting a polar ion passage into a narrow hydrophobic pore. Because the amino acids involved in the uptake, transport, and gating are all conserved within the entire CorA family, we believe this mechanism is general for the whole family including the eukaryotic homologs.
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