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Journal Article

Cryo-EM structure of Neurospora crassa respiratory complex IV

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Bausewein,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Bausewein, T., Nussberger, S., & Kühlbrandt, W. (2019). Cryo-EM structure of Neurospora crassa respiratory complex IV. IUCrJ, 6(4), 773-780. doi:10.1107/S2052252519007486.


Cite as: https://hdl.handle.net/21.11116/0000-0004-7790-3
Abstract
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 Neurospora crassa in lipid nanodiscs as cytochrome c 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 Saccharomyces cerevisiae. Its ten subunits are conserved in S. cerevisiae and Bos taurus, 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 N. crassa.