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TitleMammalian Respiratory Complex I Through the Lens of Cryo-EM.
Journal, issue, pagesAnnu Rev Biophys, Vol. 48, Page 165-184, Year 2019
Publish dateMay 6, 2019
AuthorsAhmed-Noor A Agip / James N Blaza / Justin G Fedor / Judy Hirst /
PubMed AbstractSingle-particle electron cryomicroscopy (cryo-EM) has led to a revolution in structural work on mammalian respiratory complex I. Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane- ...Single-particle electron cryomicroscopy (cryo-EM) has led to a revolution in structural work on mammalian respiratory complex I. Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane-bound redox-driven proton pump, is one of the largest and most complicated enzymes in the mammalian cell. Rapid progress, following the first 5-Å resolution data on bovine complex I in 2014, has led to a model for mouse complex I at 3.3-Å resolution that contains 96% of the 8,518 residues and to the identification of different particle classes, some of which are assigned to biochemically defined states. Factors that helped improve resolution, including improvements to biochemistry, cryo-EM grid preparation, data collection strategy, and image processing, are discussed. Together with recent structural data from an ancient relative, membrane-bound hydrogenase, cryo-EM on mammalian complex I has provided new insights into the proton-pumping machinery and a foundation for understanding the enzyme's catalytic mechanism.
External linksAnnu Rev Biophys / PubMed:30786232
MethodsEM (single particle)
Resolution4.1 Å
Structure data

EMDB-0151:
Rhesus macaque mitochondrial complex I
Method: EM (single particle) / Resolution: 4.1 Å

Source
  • Macaca mulatta (Rhesus monkey)

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