ArticleThe Biochemical journal2013
Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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26 citing papers in PubMed, 51 citations in OpenAlex.
- How mutagenesis and laboratory conditions affect the genome of the metal-resistant bacteriumJournal of bacteriology · 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
- Investigating the mechanism of aluminum resistance conferred by aluminum resistance protein 1.Protein science : a publication of the Protein Society · 2026Article
- Structure and function of the human mitochondrial MRS2 channel.Nature structural & molecular biology · 2025Article
- 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
- Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms.Nature communications · 2023Article
- Conformation-specific Synthetic Antibodies Discriminate Multiple Functional States of the Ion Channel CorA.Journal of molecular biology · 2023Article
- Molecular basis of MgNature communications · 2023Article
- Purification and Characterization of a DegP-Type Protease from the Marine BacteriumMicroorganisms · 2023Article
- The human MRS2 magnesium-binding domain is a regulatory feedback switch for channel activity.Life science alliance · 2023Article
- Structural and functional comparison of magnesium transporters throughout evolution.Cellular and molecular life sciences : CMLS · 2022Review
- MgeLife · 2022Article
- Asymmetric CorA Gating Mechanism as Observed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2021Article
- Cation permeability in CorA family of proteins.Scientific reports · 2020Article
- Article
- Loss of cytosolic MgBiochimica et biophysica acta. General subjects · 2019Article
- The structural basis of proton driven zinc transport by ZntB.Nature communications · 2017Article
- Comparative genomic analyses of transport proteins encoded within the red algae Chondrus crispus, Galdieria sulphuraria, and Cyanidioschyzon merolaeJournal of phycology · 2017Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CorA family of divalent cation transporters utilizes Mg2+ and Co2+ as primary substrates. The molecular mechanism of its function, including ion selectivity and gating, has not been fully characterized. Recently we reported a new structure of a CorA homologue from Methanocaldococcus jannaschii, which provided novel structural details that offered the conception of a unique gating mechanism involving conversion of an open hydrophilic gate into a closed hydrophobic one. In the present study we report functional evidence for this novel gating mechanism in the Thermotoga maritima CorA together with an improved crystal structure of this CorA to 2.7 Å (1 Å=0.1 nm) resolution. The latter reveals the organization of the selectivity filter to be similar to that of M. jannaschii CorA and also the previously unknown organization of the second signature motif of the CorA family. The proposed gating is achieved by a helical rotation upon the binding of a metal ion substrate to the regulatory binding sites. Additionally, our data suggest that the preference of this CorA for Co2+ over Mg2+ is controlled by the presence of threonine side chains in the channel. Finally, the roles of the intracellular metal-binding sites have been assigned to increased thermostability and regulation of the gating. These mechanisms most likely apply to the entire CorA family as they are regulated by the highly conserved amino acids.
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