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TitleCryo-EM structure of a mitochondrial calcium uniporter.
Journal, issue, pagesScience, Vol. 361, Issue 6401, Page 506-511, Year 2018
Publish dateAug 3, 2018
AuthorsJiho Yoo / Mengyu Wu / Ying Yin / Mark A Herzik / Gabriel C Lander / Seok-Yong Lee /
PubMed AbstractCalcium 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 linksScience / PubMed:29954988 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

EMDB-8911, PDB-6dt0:
Cryo-EM structure of a mitochondrial calcium uniporter
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • neurospora crassa (fungus)
KeywordsTRANSPORT PROTEIN / mitochondrial calcium uniporter / calcium-selective ion channel / calcium uptake / uniporter

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