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- EMDB-32203: Matrix arm of active state CI from Rotenone dataset -

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Basic information

Entry
Database: EMDB / ID: EMD-32203
TitleMatrix arm of active state CI from Rotenone dataset
Map data
Sample
  • Complex: Respiratory complex I
    • Protein or peptide: x 18 types
  • Ligand: x 11 types
Keywordsmammalian / mitochondrial / respiratory / complex I / ELECTRON TRANSPORT
Function / homology
Function and homology information


RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Mitochondrial protein degradation / oxidoreductase activity, acting on NAD(P)H / cardiac muscle tissue development / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / : ...RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Mitochondrial protein degradation / oxidoreductase activity, acting on NAD(P)H / cardiac muscle tissue development / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / negative regulation of intrinsic apoptotic signaling pathway / ATP synthesis coupled electron transport / quinone binding / : / respiratory electron transport chain / reactive oxygen species metabolic process / electron transport chain / negative regulation of cell growth / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / nuclear body / mitochondrion / membrane / metal ion binding / cytosol
Similarity search - Function
NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / : / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / Zinc finger, CHCC-type / Zinc-finger domain / GRIM-19 ...NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / : / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / Zinc finger, CHCC-type / Zinc-finger domain / GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / : / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH-quinone oxidoreductase subunit 3, ferredoxin-like domain / SLBB domain / : / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / Complex 1 LYR protein domain / Complex 1 protein (LYR family) / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / : / NADH-quinone oxidoreductase, subunit D / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / NADH dehydrogenase, subunit C / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NAD-dependent epimerase/dehydratase / NuoE domain / NAD dependent epimerase/dehydratase family / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH-quinone oxidoreductase subunit E-like / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / [NiFe]-hydrogenase, large subunit / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Acyl carrier protein (ACP) / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Phosphopantetheine attachment site / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / Phosphopantetheine attachment site. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Thioredoxin-like superfamily / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / Acyl carrier protein ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig) / pig (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsGu JK / Yang MJ
Funding support China, 3 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFA0504600 and 2016YFA0501100 China
National Natural Science Foundation of China (NSFC)31625008 China
National Natural Science Foundation of China (NSFC)32030056, 21532004 and 31570733 and 31800620 China
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: The coupling mechanism of mammalian mitochondrial complex I.
Authors: Jinke Gu / Tianya Liu / Runyu Guo / Laixing Zhang / Maojun Yang /
Abstract: Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in ...Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in mitochondria. In the present study, we report cryo-electron microscopy structures of CI from Sus scrofa in six treatment conditions at a resolution of 2.4-3.5 Å, in which CI structures of each condition can be classified into two biochemical classes (active or deactive), with a notably higher proportion of active CI particles. These structures illuminate how hydrophobic ubiquinone-10 (Q10) with its long isoprenoid tail is bound and reduced in a narrow Q chamber comprising four different Q10-binding sites. Structural comparisons of active CI structures from our decylubiquinone-NADH and rotenone-NADH datasets reveal that Q10 reduction at site 1 is not coupled to proton pumping in the membrane arm, which might instead be coupled to Q10 oxidation at site 2. Our data overturn the widely accepted previous proposal about the coupling mechanism of CI.
History
DepositionNov 14, 2021-
Header (metadata) releaseNov 23, 2022-
Map releaseNov 23, 2022-
UpdateJun 28, 2023-
Current statusJun 28, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32203.png

Downloads & links

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Map

FileDownload / File: emd_32203.map.gz / Format: CCP4 / Size: 113.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 310 pix.
= 333.002 Å		1.07 Å/pix.
x 310 pix.
= 333.002 Å		1.07 Å/pix.
x 310 pix.
= 333.002 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.0742 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0309
Minimum - Maximum-0.11219774 - 0.2004557
Average (Standard dev.)0.00024143395 (±0.004928624)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions310310310
Spacing310310310
CellA=B=C: 333.002 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Respiratory complex I

EntireName: Respiratory complex I
Components
  • Complex: Respiratory complex I
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: Acyl carrier protein, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: (2R,6aS,12aS)-8,9-dimethoxy-2-(prop-1-en-2-yl)-1,2,12,12a-tetrahydrofuro[2',3':7,8][1]benzopyrano[2,3-c][1]benzopyran-6(6aH)-one
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: MAGNESIUM ION
  • Ligand: CARDIOLIPIN
  • Ligand: ZINC ION

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Supramolecule #1: Respiratory complex I

SupramoleculeName: Respiratory complex I / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Source (natural)Organism: Sus scrofa (pig)

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Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 47.434066 KDa
SequenceString: APKKTSFGSL KDEDRIFTNL YGRHDWRLKG AQSRGDWYKT KEILLKGPDW ILGEVKTSGL RGRGGAGFPT GLKWSFMNKP SDGRPKYLV VNADEGEPGT CKDREIIRHD PHKLVEGCLV GGRAMGARAA YIYIRGEFYN EASNLQVAIR EAYEAGLIGK N ACGSGYDF ...String:
APKKTSFGSL KDEDRIFTNL YGRHDWRLKG AQSRGDWYKT KEILLKGPDW ILGEVKTSGL RGRGGAGFPT GLKWSFMNKP SDGRPKYLV VNADEGEPGT CKDREIIRHD PHKLVEGCLV GGRAMGARAA YIYIRGEFYN EASNLQVAIR EAYEAGLIGK N ACGSGYDF DVFVVRGAGA YICGEETALI ESIEGKQGKP RLKPPFPADV GVFGCPTTVA NVETVAVSPT ICRRGGAWFA SF GRERNSG TKLFNISGHV NHPCTVEEEM SVPLKELIEK HAGGVIGGWD NLLAVIPGGS STPLIPKSVC ETVLMDFDAL VQA QTGLGT AAVIVMDRST DIVKAIARLI EFYKHESCGQ CTPCREGVDW MNKVMARFVK GDARPAEIDS LWEISKQIEG HTIC ALGDG AAWPVQGLIR HFRPELEERM QQFALQHQ

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Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 20.207957 KDa
SequenceString:
TYKFVNMREP SMDMKSVTDR AAQTLLWTEL VRGLGMTLSY LFREPATINY PFEKGPLSPR FRGEHALRRY PSGEERCIAC KLCEAVCPA QAITIEAEPR ADGSRRTTRY DIDMTKCIYC GFCQEACPVD AIVEGPNFEF STETHEELLY NKEKLLNNGD K WEAEIAAN IQADYLYR

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Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 17.874953 KDa
SequenceString:
SRGEYVVAKL DDLVNWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRFG VVFRASPRQS DVMIVAGTLT NKMAPALRKV YDQMPEPRY VVSMGSCANG GGYYHYSYSV VRGCDRIVPV DIYVPGCPPT AEALLYGILQ LQRKIKREKR LRIWYRR

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Macromolecule #4: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 13.812977 KDa
SequenceString:
GTSVKPIFSR DMNEAKRRVR ELYRAWYREV PNTVHLFQLD ISVKQGRDKV REMFMKNAHV TDPRVVDLLV IKGKMELEET INVWKQRTH IMRFFHETEA PRPTDFLSKF YVGHDP

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Macromolecule #5: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 9.84128 KDa
SequenceString:
LGLREIRIHL CQRSPGSQGV RDFIEKRYVE LKKANPDLPI LIRECSDVQP KLWARYAFGQ EKNVSLNNFS ADQVTRTLEN VLSGKA

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Macromolecule #6: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 10.133566 KDa
SequenceString:
SDAPPLTLEA IKDRVLYVLK LYDKIDPEKL SVNSHFMKDL GLDSLDQVEI IMAMEDEFGF EIPDIDAEKL MCPQEIVDYI ADKKDVYE

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Macromolecule #7: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 12.949106 KDa
SequenceString:
LKKTTGLVGL AVCETPHERL KILYTKILDV LGQIPKNAAY RKYTEQITNE KLGMVKAEPD VKKLEEQLQG GQIEEVILQA ENELSLARK MLRWKPWEPL VEEPPANQWK WPI

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Macromolecule #8: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 12.517394 KDa
SequenceString:
ASATRVIQLL RNWASGRDLQ AKLQLRYQEI SKRTQPPPKL PVGPSHKLSN NYYCTRDGRR EAMPPSIVMS SQKVLASGKP AESSAVAET EKKAVTPAPP IKRWELSKDQ PYL

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Macromolecule #9: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitoc...

MacromoleculeName: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 38.954051 KDa
SequenceString: LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP ...String:
LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP SDIFGREDRF LNYFASMRWF GGVPLISLGK ETVKQPVYIV DVSKGIINAI KDPDAKGKTF AFVGPNRYLL FD LVQYIFA VAYRPFLPYP LPHFAYRWVG RLFEVSPFEP WTTRDKVERV HMSDMTLPHL PGLEDLGIQA TPLELKAIEV LRR HRTYRW LTSEMEDVKP AKTVNI

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Macromolecule #10: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 5.193683 KDa
SequenceString:
FDNSTYRNLQ HHEYSTYTFL DLNVELSKFR MPQPSSGRQS PRH

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Macromolecule #11: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 14.442389 KDa
SequenceString:
QLIAVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQSG VNNTKKWKME FDTRERWENP LMGWSSTADP LSNLVLTFST KEDAVAFAE KNGWSFDVEE RKVPKPKSKS YGANFSWNKR TRVSTK

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Macromolecule #12: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 75.770773 KDa
SequenceString: SNLIEVFVDG QSVMVEPGTT VLQACEKVGM QIPRFCYHER LSVAGNCRMC LVEIEKAPKV VAACAMPVMK GWNILTNSEK SKKAREGVM EFLLANHPLD CPICDQGGEC DLQDQSMMFG SDRSRFLEGK RAVEDKNIGP LVKTIMTRCI QCTRCIRFAS E IAGVDDLG ...String:
SNLIEVFVDG QSVMVEPGTT VLQACEKVGM QIPRFCYHER LSVAGNCRMC LVEIEKAPKV VAACAMPVMK GWNILTNSEK SKKAREGVM EFLLANHPLD CPICDQGGEC DLQDQSMMFG SDRSRFLEGK RAVEDKNIGP LVKTIMTRCI QCTRCIRFAS E IAGVDDLG TTGRGNDMQV GTYIEKMFMS ELSGNIIDIC PVGALTSKPY AFTARPWETR KTESIDVMDA VGSNIVVSTR TG EVMRILP RMHEDINEEW ISDKTRFAYD GLKRQRLTQP MIRNEKGLLT YTTWEDALSR VAGMLQSFQG NDVAAIAGGL VDA EALVAL KDLLNRVDSD SLCTEEVFPT AGAGTDLRSN YLLNTTIAGV EEADVILLVG TNPRFEAPLF NARIRKSWLH NDLK VALIG SPVDLTYRYD HLGDSPKILQ DIASGNHPFS QILKEAKKPM VVLGSSALQR SDGTAILAAV SNIAQNIRLS SGVTG DWKV MNILHRIASQ VAALDLGYKP GVEAIRKNPP KVLFLLGADG GCITRQDLPK DCFIIYQGHH GDVGAPMADV ILPGAA YTE KSATYVNTEG RAQQTKVAVT PPGLAREDWK IIRALSEIAG MTLPYDTLDQ VRSRLEEVSP NLVRYDDVEG ANYFQQA NE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGI

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Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 17.031244 KDa
SequenceString:
ELVQVLRRGL QQVSGHGGLR GYLRVLFRAN DVRVGTLVGE DKYGNKYYED NKQFFGRHRW VIYTTEMNGR DTFWDVDGSM VPPEWHRWL HCMTDDPPTT KPPTARKYIW TNHKFNVSGT PQQYVPYSTT RKKIQEWVPP STPYK

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Macromolecule #14: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 23.826336 KDa
SequenceString: GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD ...String:
GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG PGFGVQAGL

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Macromolecule #15: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 24.52173 KDa
SequenceString: TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL ...String:
TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL RYDDEVKRVV AEPVELAQEF RKFDLNSPWE AFPAYRQPPE

+
Macromolecule #16: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 44.127691 KDa
SequenceString: SNLTLNFGPQ HPAAHGVLRL VMELSGEMVR KCDPHIGLLH (2MR)GTEKLIEYK TYLQALPYFD RLDYVSMMCN EQAYSL AVE KLLNIQPPPR AQWIRVLFGE ITRLLNHIMA VTTHALDIGA MTPFFWMFEE REKMFEFYER VSGARMHAAY IRPGGVH QD LPLGLLDDIY ...String:
SNLTLNFGPQ HPAAHGVLRL VMELSGEMVR KCDPHIGLLH (2MR)GTEKLIEYK TYLQALPYFD RLDYVSMMCN EQAYSL AVE KLLNIQPPPR AQWIRVLFGE ITRLLNHIMA VTTHALDIGA MTPFFWMFEE REKMFEFYER VSGARMHAAY IRPGGVH QD LPLGLLDDIY EFSKNFSFRI DELEEMLTNN RIWRNRTVDI GVVTAEDALN YGFSGVMLRG SGIQWDLRKT QPYDVYDQ V EFDVPIGSRG DCYDRYLCRV EEMRQSLRII SQCLNKMPPG EIKVDDAKVS PPKRAEMKTS MESLIHHFKL YTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR

+
Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 10.567635 KDa
SequenceString:
GVRTSPTGEK VTHTGQAYDD GDYRRVRFSD RQKEVNENFA IDLIAEQPVS EVGSRVISCD GGGGALGHPR VYINLDKETK TGTCGYCGL QFRQPHH

+
Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 3.204705 KDa
SequenceString:
ASKVKQDMPP PGGYGPIDYK RNLPRRGLS

+
Macromolecule #19: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 19 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

+
Macromolecule #20: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 20 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

+
Macromolecule #21: (2R,6aS,12aS)-8,9-dimethoxy-2-(prop-1-en-2-yl)-1,2,12,12a-tetrahy...

MacromoleculeName: (2R,6aS,12aS)-8,9-dimethoxy-2-(prop-1-en-2-yl)-1,2,12,12a-tetrahydrofuro[2',3':7,8][1]benzopyrano[2,3-c][1]benzopyran-6(6aH)-one
type: ligand / ID: 21 / Number of copies: 1 / Formula: 970
Molecular weightTheoretical: 394.417 Da
Chemical component information

ChemComp-970:
(2R,6aS,12aS)-8,9-dimethoxy-2-(prop-1-en-2-yl)-1,2,12,12a-tetrahydrofuro[2',3':7,8][1]benzopyrano[2,3-c][1]benzopyran-6(6aH)-one

+
Macromolecule #22: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 22 / Number of copies: 1 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

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Macromolecule #23: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 23 / Number of copies: 1 / Formula: PEE
Molecular weightTheoretical: 744.034 Da
Chemical component information

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

+
Macromolecule #24: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 24 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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Macromolecule #25: Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer

MacromoleculeName: Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer / type: ligand / ID: 25 / Number of copies: 1 / Formula: UQ
Molecular weightTheoretical: 863.343 Da
Chemical component information

ChemComp-UQ:
Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer

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Macromolecule #26: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 26 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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Macromolecule #27: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 27 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #28: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 28 / Number of copies: 1 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

+
Macromolecule #29: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 29 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 111024
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: RANDOM ASSIGNMENT

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