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6YMY

Cytochrome c oxidase from Saccharomyces cerevisiae

Summary for 6YMY
Entry DOI10.2210/pdb6ymy/pdb
EMDB information10848
DescriptorCytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 12, mitochondrial, Cytochrome c oxidase subunit 13, mitochondrial, ... (19 entities in total)
Functional Keywordsciv, cytco, electron transport
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
More
Total number of polymer chains12
Total formula weight209312.70
Authors
Berndtsson, J.,Rathore, S.,Ott, M. (deposition date: 2020-04-10, release date: 2020-09-09, Last modification date: 2024-10-23)
Primary citationBerndtsson, J.,Aufschnaiter, A.,Rathore, S.,Marin-Buera, L.,Dawitz, H.,Diessl, J.,Kohler, V.,Barrientos, A.,Buttner, S.,Fontanesi, F.,Ott, M.
Respiratory supercomplexes enhance electron transport by decreasing cytochrome c diffusion distance.
Embo Rep., 21:e51015-e51015, 2020
Cited by
PubMed Abstract: Respiratory chains are crucial for cellular energy conversion and consist of multi-subunit complexes that can assemble into supercomplexes. These structures have been intensively characterized in various organisms, but their physiological roles remain unclear. Here, we elucidate their function by leveraging a high-resolution structural model of yeast respiratory supercomplexes that allowed us to inhibit supercomplex formation by mutation of key residues in the interaction interface. Analyses of a mutant defective in supercomplex formation, which still contains fully functional individual complexes, show that the lack of supercomplex assembly delays the diffusion of cytochrome c between the separated complexes, thus reducing electron transfer efficiency. Consequently, competitive cellular fitness is severely reduced in the absence of supercomplex formation and can be restored by overexpression of cytochrome c. In sum, our results establish how respiratory supercomplexes increase the efficiency of cellular energy conversion, thereby providing an evolutionary advantage for aerobic organisms.
PubMed: 33016568
DOI: 10.15252/embr.202051015
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.41 Å)
Structure validation

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