ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation.
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 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed.
- 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
- 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
- Mrs2-mediated mitochondrial magnesium uptake is essential for the regulation of MCU-mediated mitochondrial CaMitochondrion · 2024Article
- Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms.International journal of molecular sciences · 2024Review
- 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
- Hyphal Growth inMicrobiology spectrum · 2023Article
- The human MRS2 magnesium-binding domain is a regulatory feedback switch for channel activity.Life science alliance · 2023Article
- Two transporters mobilize magnesium from vacuolar stores to enable plant acclimation to magnesium deficiency.Plant physiology · 2022Article
- MgeLife · 2022Article
- Ion selectivity and gating behavior of the CorA-type channel Bpss1228.Frontiers in chemistry · 2022Article
- Asymmetric CorA Gating Mechanism as Observed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2021Article
- Article
- Article
- Loss of cytosolic MgBiochimica et biophysica acta. General subjects · 2019Article
- The structural basis of proton driven zinc transport by ZntB.Nature communications · 2017Article
- Mutations in the ArabidopsisFrontiers in plant science · 2017Article
- Current state of theoretical and experimental studies of the voltage-dependent anion channel (VDAC).Biochimica et biophysica acta · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Magnesium ions (Mg(2+)) are essential for life, but the mechanisms regulating their transport into and out of cells remain poorly understood. The CorA-Mrs2-Alr1 superfamily of Mg(2+) channels represents the most prevalent group of proteins enabling Mg(2+) ions to cross membranes. Thermotoga maritima CorA (TmCorA) is the only member of this protein family whose complete 3D fold is known. Here, we report the crystal structure of a mutant in the presence and absence of divalent ions and compare it with previous divalent ion-bound TmCorA structures. With Mg(2+) present, this structure shows binding of a hydrated Mg(2+) ion to the periplasmic Gly-Met-Asn (GMN) motif, revealing clues of ion selectivity in this unique channel family. In the absence of Mg(2+), TmCorA displays an unexpected asymmetric conformation caused by radial and lateral tilts of protomers that leads to bending of the central, pore-lining helix. Molecular dynamics simulations support these movements, including a bell-like deflection. Mass spectrometric analysis confirms that major proteolytic cleavage occurs within a region that is selectively exposed by such a bell-like bending motion. Our results point to a sequential allosteric model of regulation, where intracellular Mg(2+) binding locks TmCorA in a symmetric, transport-incompetent conformation and loss of intracellular Mg(2+) causes an asymmetric, potentially influx-competent conformation of the channel.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.