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3JCG

Cryo-EM structure of the magnesium channel CorA in the magnesium-free, asymmetric open state I

Summary for 3JCG
Entry DOI10.2210/pdb3jcg/pdb
Related3JCF 3JCH
EMDB information6551 6552 6553
DescriptorMagnesium transport protein CorA (1 entity in total)
Functional Keywordsmembrane protein, ion channel, magnesium channel, pentameric complex, symmetry vs. asymmetry, conformational change, gating mechanism, direct electron detector, k2, transport protein
Biological sourceThermotoga maritima
Total number of polymer chains5
Total formula weight207490.41
Authors
Matthies, D.,Perozo, E.,Subramaniam, S. (deposition date: 2015-12-11, release date: 2016-02-17, Last modification date: 2024-02-21)
Primary citationMatthies, 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: 26871634
DOI: 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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