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- EMDB-0262: III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae -

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Basic information

Entry
Database: EMDB / ID: EMD-0262
TitleIII2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae
Map dataThe sharpened map of the III2IV2 supercomplex
Sample
  • Complex: III2-IV2 mitochondrial respiratory supercomplex
    • Complex: 10-subunit yeast cytochrome bc1
      • Protein or peptide: x 10 types
    • Complex: 12-subunit cytochrome c oxidase with isoform Cox5A
      • Protein or peptide: x 12 types
Function / homology
Function and homology information


mitochondrial cytochrome c oxidase assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / Respiratory electron transport / mitochondrial respirasome assembly / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / mitochondrial respirasome / cytochrome-c oxidase ...mitochondrial cytochrome c oxidase assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / Respiratory electron transport / mitochondrial respirasome assembly / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / mitochondrial respirasome / cytochrome-c oxidase / quinol-cytochrome-c reductase / cellular respiration / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / electron transport coupled proton transport / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial crista / ATP synthesis coupled electron transport / enzyme regulator activity / aerobic respiration / proton transmembrane transport / nuclear periphery / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / proteolysis / zinc ion binding / metal ion binding / cytosol
Similarity search - Function
Cytochrome c oxidase subunit VII, budding yeast / Cytochrome c oxidase, subunit VIIa, fungal / Cytochrome b-c1 complex subunit 10, fungi / Ubiquinol-cytochrome-c reductase complex subunit (QCR10) / : / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase subunit VIIc superfamily ...Cytochrome c oxidase subunit VII, budding yeast / Cytochrome c oxidase, subunit VIIa, fungal / Cytochrome b-c1 complex subunit 10, fungi / Ubiquinol-cytochrome-c reductase complex subunit (QCR10) / : / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase subunit VIIc superfamily / Cytochrome c oxidase subunit IV superfamily / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit Va/VI / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase subunit Va / Cytochrome c oxidase, subunit VIb / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase subunit I domain / Cytochrome c oxidase, subunit II / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Cytochrome c oxidase subunit III-like superfamily / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome b / : / : / Cytochrome c/quinol oxidase subunit II / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Di-haem cytochrome, transmembrane / Cytochrome C oxidase subunit II, periplasmic domain / Rieske iron-sulphur protein / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily
Similarity search - Domain/homology
Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 2 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5A, mitochondrial / Cytochrome c oxidase subunit 6, mitochondrial / Cytochrome c oxidase subunit 4, mitochondrial / Cytochrome c oxidase subunit 8, mitochondrial ...Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 2 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5A, mitochondrial / Cytochrome c oxidase subunit 6, mitochondrial / Cytochrome c oxidase subunit 4, mitochondrial / Cytochrome c oxidase subunit 8, mitochondrial / Cytochrome c1, heme protein, mitochondrial / Cytochrome c oxidase subunit 9, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 8, mitochondrial / Cytochrome c oxidase subunit 7, mitochondrial / Cytochrome b-c1 complex subunit 9, mitochondrial / Cytochrome c oxidase subunit 13, mitochondrial / Cytochrome b-c1 complex subunit 10, mitochondrial / Cytochrome c oxidase subunit 12, mitochondrial / Cytochrome c oxidase subunit 26, mitochondrial
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.31 Å
AuthorsHartley AM / Lukoyanova N / Pinotsis N / Marechal A
CitationJournal: Nat Struct Mol Biol / Year: 2019
Title: Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc.
Authors: Andrew M Hartley / Natalya Lukoyanova / Yunyi Zhang / Alfredo Cabrera-Orefice / Susanne Arnold / Brigitte Meunier / Nikos Pinotsis / Amandine Maréchal /
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 ...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.
History
DepositionSep 27, 2018-
Header (metadata) releaseOct 10, 2018-
Map releaseDec 26, 2018-
UpdateFeb 27, 2019-
Current statusFeb 27, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6hu9
  • Surface level: 0.0263
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0262.png

Downloads & links

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Map

FileDownload / File: emd_0262.map.gz / Format: CCP4 / Size: 113.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe sharpened map of the III2IV2 supercomplex
Voxel sizeX=Y=Z: 1.3861 Å
Density
Contour LevelBy AUTHOR: 0.0263 / Movie #1: 0.035
Minimum - Maximum-0.14692926 - 0.2550798
Average (Standard dev.)0.0005225369 (±0.009231779)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions310310310
Spacing310310310
CellA=B=C: 429.691 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.38611.38611.3861
M x/y/z310310310
origin x/y/z0.0000.0000.000
length x/y/z429.691429.691429.691
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS310310310
D min/max/mean-0.1470.2550.001

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Supplemental data

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Sample components

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Entire : III2-IV2 mitochondrial respiratory supercomplex

EntireName: III2-IV2 mitochondrial respiratory supercomplex
Components
  • Complex: III2-IV2 mitochondrial respiratory supercomplex
    • Complex: 10-subunit yeast cytochrome bc1
      • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
      • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
      • Protein or peptide: Cytochrome b
      • Protein or peptide: Cytochrome c1, heme protein, mitochondrial
      • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
      • Protein or peptide: Cytochrome b-c1 complex subunit 6
      • Protein or peptide: Cytochrome b-c1 complex subunit 7
      • Protein or peptide: Cytochrome b-c1 complex subunit 8
      • Protein or peptide: Cytochrome b-c1 complex subunit 9
      • Protein or peptide: Cytochrome b-c1 complex subunit 10
    • Complex: 12-subunit cytochrome c oxidase with isoform Cox5A
      • Protein or peptide: Cox1
      • Protein or peptide: Cox2Cytochrome c oxidase subunit 2
      • Protein or peptide: Cox3
      • Protein or peptide: Cox4
      • Protein or peptide: Cox5A
      • Protein or peptide: Cox6
      • Protein or peptide: Cox7
      • Protein or peptide: Cox8
      • Protein or peptide: Cox9
      • Protein or peptide: Cox12
      • Protein or peptide: Cox13
      • Protein or peptide: Cox26

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Supramolecule #1: III2-IV2 mitochondrial respiratory supercomplex

SupramoleculeName: III2-IV2 mitochondrial respiratory supercomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: W303-1B

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Supramolecule #2: 10-subunit yeast cytochrome bc1

SupramoleculeName: 10-subunit yeast cytochrome bc1 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#10
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: W303-1B

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Supramolecule #3: 12-subunit cytochrome c oxidase with isoform Cox5A

SupramoleculeName: 12-subunit cytochrome c oxidase with isoform Cox5A / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #11-#22

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Macromolecule #1: Cytochrome b-c1 complex subunit 1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: AEVTQLSNGI VVATEHNPSA HTASVGVVFG SGAANENPYN NGVSNLWKNI FLSKENSAVA AKEGLALSSN ISRDFQSYIV SSLPGSTDKS LDFLNQSFIQ QKANLLSSSN FEATKKSVLK QVQDFEENDH PNRVLEHLHS TAFQNTPLSL PTRGTLESLE NLVVADLESF ...String:
AEVTQLSNGI VVATEHNPSA HTASVGVVFG SGAANENPYN NGVSNLWKNI FLSKENSAVA AKEGLALSSN ISRDFQSYIV SSLPGSTDKS LDFLNQSFIQ QKANLLSSSN FEATKKSVLK QVQDFEENDH PNRVLEHLHS TAFQNTPLSL PTRGTLESLE NLVVADLESF ANNHFLNSNA VVVGTGNIKH EDLVNSIESK NLSLQTGTKP VLKKKAAFLG SEVRLRDDTL PKAWISLAVE GEPVNSPNYF VAKLAAQIFG SYNAFEPASR LQGIKLLDNI QEYQLCDNFN HFSLSYKDSG LWGFSTATRN VTMIDDLIHF TLKQWNRLTI SVTDTEVERA KSLLKLQLGQ LYESGNPVND ANLLGAEVLI KGSKLSLGEA FKKIDAITVK DVKAWAGKRL WDQDIAIAGT GQIEGLLDYM RIRSDMSMMR W

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Macromolecule #2: Cytochrome b-c1 complex subunit 2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: LTVSARDAPT KISTLAVKVH GGSRYATKDG VAHLLNRFNF QNTNTRSALK LVRESELLGG TFKSTLDREY ITLKATFLKD DLPYYVNALA DVLYKTAFKP HELTESVLPA ARYDYAVAEQ CPVKSAEDQL YAITFRKGLG NPLLYDGVER VSLQDIKDFA DKVYTKENLE ...String:
LTVSARDAPT KISTLAVKVH GGSRYATKDG VAHLLNRFNF QNTNTRSALK LVRESELLGG TFKSTLDREY ITLKATFLKD DLPYYVNALA DVLYKTAFKP HELTESVLPA ARYDYAVAEQ CPVKSAEDQL YAITFRKGLG NPLLYDGVER VSLQDIKDFA DKVYTKENLE VSGENVVEAD LKRFVDESLL STLPAGKSLV SKSEPKFFLG EENRVRFIGD SVAAIGIPVN KASLAQYEVL ANYLTSALSE LSGLISSAKL DKFTDGGLFT LFVRDQDSAV VSSNIKKIVA DLKKGKDLSP AINYTKLKNA VQNESVSSPI ELNFDAVKDF KLGKFNYVAV GDVSNLPYLD EL

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Macromolecule #3: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM AMHYSSNIEL AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG LYYGSYRSPR VTLWNVGVII FILTIATAFL GYCCVYGQMS HWGATVITNL FSAIPFVGND IVSWLWGGFS ...String:
MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM AMHYSSNIEL AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG LYYGSYRSPR VTLWNVGVII FILTIATAFL GYCCVYGQMS HWGATVITNL FSAIPFVGND IVSWLWGGFS VSNPTIQRFF ALHYLVPFII AAMVIMHLMA LHIHGSSNPL GITGNLDRIP MHSYFIFKDL VTVFLFMLIL ALFVFYSPNT LGHPDNYIPG NPLVTPASIV PEWYLLPFYA ILRSIPDKLL GVITMFAAIL VLLVLPFTDR SVVRGNTFKV LSKFFFFIFV FNFVLLGQIG ACHVEVPYVL MGQIATFIYF AYFLIIVPVI STIENVLFYI GRVNK

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Macromolecule #4: Cytochrome c1, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1, heme protein, mitochondrial / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MTAAEHGLHA PAYAWSHNGP FETFDHASIR RGYQVYREVC AACHSLDRVA WRTLVGVSHT NEEVRNMAEE FEYDDEPDEQ GNPKKRPGKL SDYIPGPYPN EQAARAANQG ALPPDLSLIV KARHGGCDYI FSLLTGYPDE PPAGVALPPG SNYNPYFPGG SIAMARVLFD ...String:
MTAAEHGLHA PAYAWSHNGP FETFDHASIR RGYQVYREVC AACHSLDRVA WRTLVGVSHT NEEVRNMAEE FEYDDEPDEQ GNPKKRPGKL SDYIPGPYPN EQAARAANQG ALPPDLSLIV KARHGGCDYI FSLLTGYPDE PPAGVALPPG SNYNPYFPGG SIAMARVLFD DMVEYEDGTP ATTSQMAKDV TTFLNWCAEP EHDERKRLGL KTVIILSSLY LLSIWVKKFK WAGIKTRKFV FNPPKPRK

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Macromolecule #5: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
KSTYRTPNFD DVLKENNDAD KGRSYAYFMV GAMGLLSSAG AKSTVETFIS SMTATADVLA MAKVEVNLAA IPLGKNVVVK WQGKPVFIRH RTPHEIQEAN SVDMSALKDP QTDADRVKDP QWLIMLGICT HLGCVPIGEA GDFGGWFCPC HGSHYDISGR IRKGPAPLNL EIPAYEFDGD KVIVG

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Macromolecule #6: Cytochrome b-c1 complex subunit 6

MacromoleculeName: Cytochrome b-c1 complex subunit 6 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MGMLELVGEY WEQLKITVVP VVAAAEDDDN EQHEEKAAEG EEKEEENGDE DEDEDEDEDD DDDDDEDEEE EEEVTDQLED LREHFKNTEE GKALVHHYEE CAERVKIQQQ QPGYADLEHK EDCVEEFFHL QHYLDTATAP RLFDKLK

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Macromolecule #7: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MPQSFTSIAR IGDYILKSPV LSKLCVPVAN QFINLAGYKK LGLKFDDLIA EENPIMQTAL RRLPEDESYA RAYRIIRAHQ TELTHHLLPR NEWIKAQEDV PYLLPYILEA EAAAKEKDEL DNIEVSK

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Macromolecule #8: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MGPPSGKTYM GWWGHMGGPK QKGITSYAVS PYAQKPLQGI FHNAVFNSFR RFKSQFLYVL IPAGIYWYWW KNGNEYNEFL YSKAGREELE RVNV

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Macromolecule #9: Cytochrome b-c1 complex subunit 9

MacromoleculeName: Cytochrome b-c1 complex subunit 9 / type: protein_or_peptide / ID: 9 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
SFSSLYKTFF KRNAVFVGTI FAGAFVFQTV FDTAITSWYE NHNKGKLWKD VKARIAAGDG DDDDE

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Macromolecule #10: Cytochrome b-c1 complex subunit 10

MacromoleculeName: Cytochrome b-c1 complex subunit 10 / type: protein_or_peptide / ID: 10 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
AYTSHLSSKT GLHFGRLSLR SLTAYAPNLM LWGGASMLGL FVFTEGWPKF QDTLYKKIPL LGPTLEDHTP PEDKPN

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Macromolecule #11: Cox1

MacromoleculeName: Cox1 / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL ...String:
MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVSGGGDPI LYEHLFWFFG HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD TRAYFTSATM IIAIPTGIKI FSWLATIHGG SIRLATPMLY AIAFLFLFTM GGLTGVALAN ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLNYNEKLA QIQFWLIFIG ANVIFFPMHF LGINGMPRRI PDYPDAFAGW NYVASIGSFI ATLSLFLFIY ILYDQLVNGL NNKVNNKSVI YNKAPDFVES NTIFNLNTVK SSSIEFLLTS PPAVHSFNTP AVQS

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Macromolecule #12: Cox2

MacromoleculeName: Cox2 / type: protein_or_peptide / ID: 12 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: DVPTPYACYF QDSATPNQEG ILELHDNIMF YLLVILGLVS WMLYTIVMTY SKNPIAYKYI KHGQTIEVIW TIFPAVILLI IAFPSFILLY LCDEVISPAM TIKAIGYQWY WKYEYSDFIN DSGETVEFES YVIPDELLEE GQLRLLDTDT SMVVPVDTHI RFVVTAADVI ...String:
DVPTPYACYF QDSATPNQEG ILELHDNIMF YLLVILGLVS WMLYTIVMTY SKNPIAYKYI KHGQTIEVIW TIFPAVILLI IAFPSFILLY LCDEVISPAM TIKAIGYQWY WKYEYSDFIN DSGETVEFES YVIPDELLEE GQLRLLDTDT SMVVPVDTHI RFVVTAADVI HDFAIPSLGI KVDATPGRLN QVSALIQREG VFYGACSELC GTGHANMPIK IEAVSLPKFL EWLNEQ

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Macromolecule #13: Cox3

MacromoleculeName: Cox3 / type: protein_or_peptide / ID: 13 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MTHLERSRHQ QHPFHMVMPS PWPIVVSFAL LSLALSTALT MHGYIGNMNM VYLALFVLLT SSILWFRDIV AEATYLGDHT MAVRKGINLG FLMFVLSEVL IFAGLFWAYF HSAMSPDVTL GACWPPVGIE AVQPTELPLL NTIILLSSGA TVTYSHHALI AGNRNKALSG ...String:
MTHLERSRHQ QHPFHMVMPS PWPIVVSFAL LSLALSTALT MHGYIGNMNM VYLALFVLLT SSILWFRDIV AEATYLGDHT MAVRKGINLG FLMFVLSEVL IFAGLFWAYF HSAMSPDVTL GACWPPVGIE AVQPTELPLL NTIILLSSGA TVTYSHHALI AGNRNKALSG LLITFWLIVI FVTCQYIEYT NAAFTISDGV YGSVFYAGTG LHFLHMVMLA AMLGVNYWRM RNYHLTAGHH VGYETTIIYT HVLDVIWLFL YVVFYWWGV

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Macromolecule #14: Cox4

MacromoleculeName: Cox4 / type: protein_or_peptide / ID: 14 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
QQKPVVKTAQ NLAEVNGPET LIGPGAKEGT VPTDLDQETG LARLELLGKL EGIDVFDTKP LDSSRKGTMK DPIIIESYDD YRYVGCTGSP AGSHTIMWLK PTVNEVARCW ECGSVYKLNP VGVPNDDHHH

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Macromolecule #15: Cox5A

MacromoleculeName: Cox5A / type: protein_or_peptide / ID: 15 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
AQTHALSNAA VMDLQSRWEN MPSTEQQDIV SKLSERQKLP WAQLTEPEKQ AVWYISYGEW GPRRPVLNKG DSSFIAKGVA AGLLFSVGLF AVVRMAGGQD AKTMNKEWQL KSDEYLKSKN ANPWGGYSQV QSK

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Macromolecule #16: Cox6

MacromoleculeName: Cox6 / type: protein_or_peptide / ID: 16 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
SDAHDEETFE EFTARYEKEF DEAYDLFEVQ RVLNNCFSYD LVPAPAVIEK ALRAARRVND LPTAIRVFEA LKYKVENEDQ YKAYLDELKD VRQELGVPLK EELFPSSS

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Macromolecule #17: Cox7

MacromoleculeName: Cox7 / type: protein_or_peptide / ID: 17 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
ANKVIQLQKI FQSSTKPLWW RHPRSALYLY PFYAIFAVAV VTPLLYIPNA IRGIKAKKA

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Macromolecule #18: Cox8

MacromoleculeName: Cox8 / type: protein_or_peptide / ID: 18 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
VHFKDGVYEN IPFKVKGRKT PYALSHFGFF AIGFAVPFVA CYVQLKK

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Macromolecule #19: Cox9

MacromoleculeName: Cox9 / type: protein_or_peptide / ID: 19 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
TIAPITGTIK RRVIMDIVLG FSLGGVMASY WWWGFHMDKI NKREKFYAEL AERKK

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Macromolecule #20: Cox12

MacromoleculeName: Cox12 / type: protein_or_peptide / ID: 20 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
ADQENSPLHT VGFDARFPQQ NQTKHCWQSY VDYHKCVNMK GEDFAPCKVF WKTYNALCPL DWIEKWDDQR EKGIFAGDIN SD

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Macromolecule #21: Cox13

MacromoleculeName: Cox13 / type: protein_or_peptide / ID: 21 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
ASSLPPNALK PAFGPPDKVA AQKFKESLMA TEKHAKDTSN MWVKISVWVA LPAIALTAVN TYFVEKEHAE HREHLKHVPD SEWPRDYEFM NIRSKPFFWG DGDKTLFWNP VVNRHIEHDD GARGSHHHHH H

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Macromolecule #22: Cox26

MacromoleculeName: Cox26 / type: protein_or_peptide / ID: 22 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MFFSQVLRSS ARAAPIKRYT GGRIGESWVI TEGRRLIPEI FQWSAVLSVC LGWPGAVYFF SKARKA

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.2
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 4.0 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 92 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
Details: 3 uL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 130000
Sample stageCooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Sampling interval: 5.0 µm / Average exposure time: 8.0 sec. / Average electron dose: 1.645 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: RELION (ver. 3.0)
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.0)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.0)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.31 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 44915
FSC plot (resolution estimation)

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