
Cryo-EM structure of a mitochondrial calcium uniporter.
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 Neurospora crassa 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.
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Related Subject Headings
- Protein Multimerization
- Protein Conformation
- Neurospora crassa
- Mutagenesis
- Models, Chemical
- General Science & Technology
- Fungal Proteins
- Cryoelectron Microscopy
- Conserved Sequence
- Calcium Channels
Citation

Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Protein Multimerization
- Protein Conformation
- Neurospora crassa
- Mutagenesis
- Models, Chemical
- General Science & Technology
- Fungal Proteins
- Cryoelectron Microscopy
- Conserved Sequence
- Calcium Channels