Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc 1
Por:
Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S., Meunier B., Pinotsis N., Maréchal A.
Publicada:
1 ene 2019
Resumen:
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 bc1 (complex III, CIII). Here, we present the cryogenic electron microscopy (cryo-EM) structure of S. cerevisiae CIV in a III2IV2 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. © 2018, The Author(s), under exclusive licence to Springer Nature America, Inc.
Filiaciones:
Institute of Structural and Molecular Biology, Birkbeck College, London, United Kingdom
Institute of Structural and Molecular Biology, University College London, London, United Kingdom
Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, Netherlands
Institute for Integrative Biology of the Cell, Université Paris-Saclay, Gif-sur-Yvette, France
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