6DT0
Cryo-EM structure of a mitochondrial calcium uniporter
Summary for 6DT0
| Entry DOI | 10.2210/pdb6dt0/pdb |
| EMDB information | 8911 |
| Descriptor | Mitochondrial calcium uniporter, CALCIUM ION (2 entities in total) |
| Functional Keywords | mitochondrial calcium uniporter, calcium-selective ion channel, calcium uptake, uniporter, transport protein |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 4 |
| Total formula weight | 211832.55 |
| Authors | Yoo, J.,Wu, M.,Yin, Y.,Herzik, M.A.J.,Lander, G.C.,Lee, S.-Y. (deposition date: 2018-06-14, release date: 2018-07-11, Last modification date: 2024-03-13) |
| Primary citation | Yoo, J.,Wu, M.,Yin, Y.,Herzik Jr., M.A.,Lander, G.C.,Lee, S.Y. Cryo-EM structure of a mitochondrial calcium uniporter. Science, 361:506-511, 2018 Cited by PubMed Abstract: Calcium transport plays an important role in regulating mitochondrial physiology and pathophysiology. The mitochondrial calcium uniporter (MCU) is a calcium-selective ion channel that is the primary mediator for calcium uptake into the mitochondrial matrix. Here, we present the cryo-electron microscopy structure of the full-length MCU from to an overall resolution of ~3.7 angstroms. Our structure reveals a tetrameric architecture, with the soluble and transmembrane domains adopting different symmetric arrangements within the channel. The conserved W-D-Φ-Φ-E-P-V-T-Y sequence motif of MCU pore forms a selectivity filter comprising two acidic rings separated by one helical turn along the central axis of the channel pore. The structure combined with mutagenesis gives insight into the basis of calcium recognition. PubMed: 29954988DOI: 10.1126/science.aar4056 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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