6DNF
Cryo-EM structure of the mitochondrial calcium uniporter MCU from the fungus Cyphellophora europaea
Summary for 6DNF
| Entry DOI | 10.2210/pdb6dnf/pdb |
| EMDB information | 7971 7972 |
| Descriptor | Mitochondrial calcium uniporter MCU, 1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL, CALCIUM ION (3 entities in total) |
| Functional Keywords | mitochondria, calcium, ion channel, eukaryotic, membrane protein |
| Biological source | Cyphellophora europaea CBS 101466 |
| Total number of polymer chains | 4 |
| Total formula weight | 164548.79 |
| Authors | Long, S.B.,Baradaran, R.,Wang, C. (deposition date: 2018-06-06, release date: 2018-07-11, Last modification date: 2024-03-13) |
| Primary citation | Baradaran, R.,Wang, C.,Siliciano, A.F.,Long, S.B. Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Nature, 559:580-584, 2018 Cited by PubMed Abstract: The mitochondrial calcium uniporter (MCU) is a highly selective calcium channel and a major route of calcium entry into mitochondria. How the channel catalyses ion permeation and achieves ion selectivity are not well understood, partly because MCU is thought to have a distinct architecture in comparison to other cellular channels. Here we report cryo-electron microscopy reconstructions of MCU channels from zebrafish and Cyphellophora europaea at 8.5 Å and 3.2 Å resolutions, respectively. In contrast to a previous report of pentameric stoichiometry for MCU, both channels are tetramers. The atomic model of C. europaea MCU shows that a conserved WDXXEP signature sequence forms the selectivity filter, in which calcium ions are arranged in single file. Coiled-coil legs connect the pore to N-terminal domains in the mitochondrial matrix. In C. europaea MCU, the N-terminal domains assemble as a dimer of dimers; in zebrafish MCU, they form an asymmetric crescent. The structures define principles that underlie ion permeation and calcium selectivity in this unusual channel. PubMed: 29995857DOI: 10.1038/s41586-018-0331-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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