8TS2
Cryo-EM structure of human MRS2 with EDTA
Summary for 8TS2
| Entry DOI | 10.2210/pdb8ts2/pdb |
| EMDB information | 41587 41588 |
| Descriptor | Magnesium transporter MRS2 homolog, mitochondrial, Soluble cytochrome b562 fusion protein (1 entity in total) |
| Functional Keywords | mitochondria, pentamer, cation channel, metal transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 277358.46 |
| Authors | He, Z.,Mount, J.W.,Zhang, J.,Yuan, P. (deposition date: 2023-08-10, release date: 2024-08-14, Last modification date: 2025-04-02) |
| Primary citation | He, Z.,Tu, Y.C.,Tsai, C.W.,Mount, J.,Zhang, J.,Tsai, M.F.,Yuan, P. Structure and function of the human mitochondrial MRS2 channel. Nat.Struct.Mol.Biol., 32:459-468, 2025 Cited by PubMed Abstract: The human mitochondrial RNA splicing 2 protein (MRS2) has been implicated in Mg transport across mitochondrial inner membranes, thus having an important role in Mg homeostasis critical for mitochondrial integrity and function. However, the molecular mechanisms underlying its fundamental channel properties such as ion selectivity and regulation remain unclear. Here we present a structural and functional investigation of MRS2. Cryo-electron microscopy structures in various ionic conditions reveal a pentameric channel architecture and the molecular basis of ion permeation and potential regulation mechanisms. Electrophysiological analyses demonstrate that MRS2 is a Ca-regulated, nonselective channel permeable to Mg, Ca, Na and K, which contrasts with its prokaryotic ortholog, CorA, operating as a Mg-gated Mg channel. Moreover, a conserved arginine ring within the pore of MRS2 functions to restrict cation movements, thus preventing the channel from collapsing the proton motive force that drives mitochondrial adenosine triphosphate synthesis. Together, our results provide a molecular framework for further understanding MRS2 in mitochondrial function and disease. PubMed: 39609651DOI: 10.1038/s41594-024-01420-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.95 Å) |
Structure validation
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