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Title | Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating. |
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Journal, issue, pages | Cell, Vol. 164, Issue 4, Page 747-756, Year 2016 |
Publish date | Feb 11, 2016 |
Authors | Doreen Matthies / Olivier Dalmas / Mario J Borgnia / Pawel K Dominik / Alan Merk / Prashant Rao / Bharat G Reddy / Shahidul Islam / Alberto Bartesaghi / Eduardo Perozo / Sriram Subramaniam / |
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+)- ...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. |
External links | Cell / PubMed:26871634 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 7.06 Å |
Structure data | EMDB-6551, PDB-3jcf: |
Chemicals | ChemComp-MG: |
Source |
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Keywords | TRANSPORT PROTEIN / membrane protein / ion channel / magnesium channel / pentameric complex / symmetry vs. asymmetry / conformational change / gating mechanism / direct electron detector / K2 |