ArticleBiochimica et biophysica acta2015
The Cryo-EM structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.
Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Magnesium Transporters as Crucial Regulators of Bacterial Survival and Pathogenicity.Microorganisms · 2026Review
- Investigating the mechanism of aluminum resistance conferred by aluminum resistance protein 1.Protein science : a publication of the Protein Society · 2026Article
- 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
- 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
- The structural basis of proton driven zinc transport by ZntB.Nature communications · 2017Article
- Article
- Identifying and Visualizing Macromolecular Flexibility in Structural Biology.Frontiers in molecular biosciences · 2016Review
- FmvB: A Francisella tularensis Magnesium-Responsive Outer Membrane Protein that Plays a Role in Virulence.PloS one · 2016Article
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
CorA channels are responsible for the uptake of essential magnesium ions by bacteria. X-ray crystal structures have been resolved for two full-length CorA channels, each in a non-conducting state with magnesium ions bound to the protein: These structures reveal a homo-pentameric quaternary structure with approximate 5-fold rotational symmetry about a central pore axis. We report the structure of the detergent solubilized Methanocaldococcus jannaschii CorA channel determined by Cryo-Electron Microscopy and Single Particle Averaging, supported by Small Angle X-ray Scattering and X-ray crystallography. This structure also shows a pentameric channel but with a highly asymmetric domain structure. The asymmetry of the domains includes differential separations between the trans-membrane segments, which reflects mechanical coupling of the cytoplasmic domain to the trans-membrane domain. This structure therefore reveals an important aspect of the gating mechanism of CorA channels by providing an indication of how the absence of magnesium ions leads to major structural changes.
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