Format

Send to

Choose Destination
Science. 2018 Jun 28. pii: eaar4056. doi: 10.1126/science.aar4056. [Epub ahead of print]

Cryo-EM structure of a mitochondrial calcium uniporter.

Author information

1
Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
2
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
3
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. seok-yong.lee@duke.edu glander@scripps.edu.
4
Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA. seok-yong.lee@duke.edu glander@scripps.edu.

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 Neurospora crassa to an overall resolution of ~3.7 Å. 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.

PMID:
29954988
DOI:
10.1126/science.aar4056

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center