ArticleCell2016
Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating.
Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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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.
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Who cites it
70 citing papers in PubMed.
- Prohibitin controls MRS2-Mediated mitochondrial MgCell reports · 2026Article
- Structural and mutational insights define ERMA as the ER MgScience advances · 2026Article
- Magnesium Transporters as Crucial Regulators of Bacterial Survival and Pathogenicity.Microorganisms · 2026Review
- Molecular bases of circadian magnesium rhythms across eukaryotes.FEBS letters · 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
- Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A strategic approach for efficient cryo-EM grid optimization using design of experiments.Journal of structural biology · 2025Article
- Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism.Nature structural & molecular biology · 2025Article
- Structure and function of the human mitochondrial MRS2 channel.Nature structural & molecular biology · 2025Article
- Computational drug development for membrane protein targets.Nature biotechnology · 2024Review
- Characterization of Complexes and Supramolecular Structures by Electron Microscopy.Advances in experimental medicine and biology · 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
- Novel Artificial Intelligence-Based Approaches for Ab Initio Structure Determination and Atomic Model Building for Cryo-Electron Microscopy.Micromachines · 2023Review
- Molecular basis of MgNature communications · 2023Article
- Efficient Bioremediation of Petroleum-Contaminated Soil by Immobilized Bacterial Agent ofBioengineering (Basel, Switzerland) · 2023Article
- Central cavity dehydration as a gating mechanism of potassium channels.Nature communications · 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
10 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
Abstract
CorA, the major Mg(2+) uptake system in prokaryotes, is gated by intracellular Mg(2+) (KD ∼ 1-2 mM). X-ray crystallographic studies of CorA show similar conformations under Mg(2+)-bound and Mg(2+)-free conditions, but EPR spectroscopic studies reveal large Mg(2+)-driven quaternary conformational changes. Here, we determined cryo-EM structures of CorA in the Mg(2+)-bound closed conformation and in two open Mg(2+)-free states at resolutions of 3.8, 7.1, and 7.1 Å, respectively. In the absence of bound Mg(2+), four of the five subunits are displaced to variable extents (∼ 10-25 Å) by hinge-like motions as large as ∼ 35° at the stalk helix. The transition between a single 5-fold symmetric closed state and an ensemble of low Mg(2+), open, asymmetric conformational states is, thus, the key structural signature of CorA gating. This mechanism is likely to apply to other structurally similar divalent ion channels.
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