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PDBsum entry 6hu9
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Oxidoreductase/electron transport
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PDB id
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6hu9
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Contents |
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431 a.a.
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352 a.a.
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385 a.a.
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247 a.a.
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185 a.a.
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75 a.a.
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126 a.a.
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93 a.a.
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57 a.a.
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76 a.a.
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534 a.a.
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236 a.a.
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269 a.a.
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121 a.a.
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133 a.a.
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102 a.a.
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59 a.a.
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47 a.a.
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55 a.a.
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77 a.a.
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113 a.a.
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45 a.a.
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 _ZN
×2
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 _CU
×2
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 _CA
×2
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 _MG
×2
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CUA
×4
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References listed in PDB file
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Key reference
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Title
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Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc1.
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Authors
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A.M.Hartley,
N.Lukoyanova,
Y.Zhang,
A.Cabrera-Orefice,
S.Arnold,
B.Meunier,
N.Pinotsis,
A.Maréchal.
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Ref.
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Nat Struct Mol Biol, 2019,
26,
78-83.
[DOI no: ]
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PubMed id
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Abstract
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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.
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