8Q8Q
Cryo-EM structure of the magnesium channel CtMrs2 in the open state
Summary for 8Q8Q
| Entry DOI | 10.2210/pdb8q8q/pdb |
| Related | 8Q8P |
| EMDB information | 18256 18257 |
| Descriptor | Magnesium channel Mrs2, (1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | magnesium channel mrs2, membrane protein |
| Biological source | Thermochaetoides thermophila |
| Total number of polymer chains | 5 |
| Total formula weight | 248833.79 |
| Authors | Gourdon, P.,Li, P. (deposition date: 2023-08-18, release date: 2024-11-27, Last modification date: 2025-03-26) |
| Primary citation | Li, P.,Liu, S.,Wallerstein, J.,Villones, R.L.E.,Huang, P.,Lindkvist-Petersson, K.,Meloni, G.,Lu, K.,Steen Jensen, K.,Liin, S.I.,Gourdon, P. Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism. Nat.Struct.Mol.Biol., 32:491-501, 2025 Cited by PubMed Abstract: The CorA/Mrs2 family of pentameric proteins are cardinal for the influx of Mg across cellular membranes, importing the cation to mitochondria in eukaryotes. Yet, the conducting and regulation mechanisms of permeation remain elusive, particularly for the eukaryotic Mrs2 members. Here, we report closed and open Mrs2 cryo-electron microscopy structures, accompanied by functional characterization. Mg flux is permitted by a narrow pore, gated by methionine and arginine residues in the closed state. Transition between the conformations is orchestrated by two pairs of conserved sensor-serving Mg-binding sites in the mitochondrial matrix lumen, located in between monomers. At lower levels of Mg, these ions are stripped, permitting an alternative, symmetrical shape, maintained by the RDLR motif that replaces one of the sensor site pairs in the open conformation. Thus, our findings collectively establish the molecular basis for selective Mg influx of Mrs2 and an auto-ligand-gating regulation mechanism. PubMed: 39609652DOI: 10.1038/s41594-024-01432-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.22 Å) |
Structure validation
Download full validation report
