+Search query
-Structure paper
Title | Cryo-EM structure of a mitochondrial calcium uniporter. |
---|---|
Journal, issue, pages | Science, Vol. 361, Issue 6401, Page 506-511, Year 2018 |
Publish date | Aug 3, 2018 |
Authors | Jiho Yoo / Mengyu Wu / Ying Yin / Mark A Herzik / Gabriel C Lander / Seok-Yong Lee / |
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 ...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. |
External links | Science / PubMed:29954988 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 Å |
Structure data | |
Chemicals | ChemComp-CA: |
Source |
|
Keywords | TRANSPORT PROTEIN / mitochondrial calcium uniporter / calcium-selective ion channel / calcium uptake / uniporter |