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-Structure paper
Title | X-ray and cryo-EM structures of the mitochondrial calcium uniporter. |
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Journal, issue, pages | Nature, Vol. 559, Issue 7715, Page 575-579, Year 2018 |
Publish date | Jul 11, 2018 |
Authors | Chao Fan / Minrui Fan / Benjamin J Orlando / Nathan M Fastman / Jinru Zhang / Yan Xu / Melissa G Chambers / Xiaofang Xu / Kay Perry / Maofu Liao / Liang Feng / |
PubMed Abstract | Mitochondrial calcium uptake is critical for regulating ATP production, intracellular calcium signalling, and cell death. This uptake is mediated by a highly selective calcium channel called the ...Mitochondrial calcium uptake is critical for regulating ATP production, intracellular calcium signalling, and cell death. This uptake is mediated by a highly selective calcium channel called the mitochondrial calcium uniporter (MCU). Here, we determined the structures of the pore-forming MCU proteins from two fungi by X-ray crystallography and single-particle cryo-electron microscopy. The stoichiometry, overall architecture, and individual subunit structure differed markedly from those described in the recent nuclear magnetic resonance structure of Caenorhabditis elegans MCU. We observed a dimer-of-dimer architecture across species and chemical environments, which was corroborated by biochemical experiments. Structural analyses and functional characterization uncovered the roles of key residues in the pore. These results reveal a new ion channel architecture, provide insights into calcium coordination, selectivity and conduction, and establish a structural framework for understanding the mechanism of mitochondrial calcium uniporter function. |
External links | Nature / PubMed:29995856 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.09608311048 - 7.0 Å |
Structure data | EMDB-7800: EMDB-7801: EMDB-7802: EMDB-7803: EMDB-7804: PDB-6c5r: PDB-6c5w: |
Chemicals | ChemComp-CA: |
Source |
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Keywords | CYTOSOLIC PROTEIN / MEMBRANE PROTEIN |