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6HU9

III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae

Summary for 6HU9
Entry DOI10.2210/pdb6hu9/pdb
EMDB information0262 0268 0269
DescriptorCytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome b-c1 complex subunit 10, Cytochrome c oxidase subunit 1, ... (35 entities in total)
Functional Keywordscytochrome c oxidase cytochrome bc1 mitochondria respiratory chain supercomplex, oxidoreductase, electron transport, oxidoreductase-electron transport complex, oxidoreductase/electron transport
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains44
Total formula weight936427.10
Authors
Hartley, A.M.,Pinotsis, N.,Marechal, A. (deposition date: 2018-10-05, release date: 2018-12-26, Last modification date: 2024-11-20)
Primary citationHartley, A.M.,Lukoyanova, N.,Zhang, Y.,Cabrera-Orefice, A.,Arnold, S.,Meunier, B.,Pinotsis, N.,Marechal, A.
Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc1.
Nat. Struct. Mol. Biol., 26:78-83, 2019
Cited by
PubMed Abstract: Cytochrome c oxidase (complex IV, CIV) is known in mammals to exist independently or in association with other respiratory proteins to form supercomplexes (SCs). In Saccharomyces cerevisiae, CIV is found solely in an SC with cytochrome bc (complex III, CIII). Here, we present the cryogenic electron microscopy (cryo-EM) structure of S. cerevisiae CIV in a IIIIV SC at 3.3 Å resolution. While overall similarity to mammalian homologs is high, we found notable differences in the supernumerary subunits Cox26 and Cox13; the latter exhibits a unique arrangement that precludes CIV dimerization as seen in bovine. A conformational shift in the matrix domain of Cox5A-involved in allosteric inhibition by ATP-may arise from its association with CIII. The CIII-CIV arrangement highlights a conserved interaction interface of CIII, albeit one occupied by complex I in mammalian respirasomes. We discuss our findings in the context of the potential impact of SC formation on CIV regulation.
PubMed: 30598554
DOI: 10.1038/s41594-018-0172-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.35 Å)
Structure validation

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