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TitleCryo-EM structure of respiratory complex IV.
Journal, issue, pagesIUCrJ, Vol. 6, Issue Pt 4, Page 773-780, Year 2019
Publish dateJul 1, 2019
AuthorsThomas Bausewein / Stephan Nussberger / Werner Kühlbrandt /
PubMed AbstractIn fungi, the mitochondrial respiratory chain complexes (complexes I-IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane ...In fungi, the mitochondrial respiratory chain complexes (complexes I-IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane protein from in lipid nanodiscs as cytochrome oxidase (complex IV) and its structure was determined at 5.5 Å resolution. The map closely resembles the cryo-EM structure of complex IV from . Its ten subunits are conserved in and , but other transmembrane subunits are missing. The different structure of the Cox5a subunit is typical for fungal complex IV and may affect the interaction with complex III in a respiratory supercomplex. Additional density was found between the matrix domains of the Cox4 and Cox5a subunits that appears to be specific to .
External linksIUCrJ / PubMed:31316820 / PubMed Central
MethodsEM (single particle)
Resolution5.5 Å
Structure data

EMDB-4720:
Neurospora crassa cytochrome C oxidase (complex IV) in lipid nanodisc
Method: EM (single particle) / Resolution: 5.5 Å

Source
  • Neurospora crassa (fungus)

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