3JCG
Cryo-EM structure of the magnesium channel CorA in the magnesium-free, asymmetric open state I
Summary for 3JCG
Entry DOI | 10.2210/pdb3jcg/pdb |
Related | 3JCF 3JCH |
EMDB information | 6551 6552 6553 |
Descriptor | Magnesium transport protein CorA (1 entity in total) |
Functional Keywords | membrane protein, ion channel, magnesium channel, pentameric complex, symmetry vs. asymmetry, conformational change, gating mechanism, direct electron detector, k2, transport protein |
Biological source | Thermotoga maritima |
Total number of polymer chains | 5 |
Total formula weight | 207490.41 |
Authors | Matthies, D.,Perozo, E.,Subramaniam, S. (deposition date: 2015-12-11, release date: 2016-02-17, Last modification date: 2024-02-21) |
Primary citation | Matthies, D.,Dalmas, O.,Borgnia, M.J.,Dominik, P.K.,Merk, A.,Rao, P.,Reddy, B.G.,Islam, S.,Bartesaghi, A.,Perozo, E.,Subramaniam, S. Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating. Cell(Cambridge,Mass.), 164:747-756, 2016 Cited by PubMed 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. PubMed: 26871634DOI: 10.1016/j.cell.2015.12.055 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (7.06 Å) |
Structure validation
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