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- EMDB-32188: Matrix arm of deactive state CI from Q10 dataset -

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Basic information

Entry
Database: EMDB / ID: EMD-32188
TitleMatrix arm of deactive state CI from Q10 dataset
Map data
Sample
  • Complex: Respiratory complex I
    • Protein or peptide: x 9 types
  • Protein or peptide: x 9 types
  • Ligand: x 10 types
Keywordsmammalian / mitochondrial / respiratory / complex I / ELECTRON TRANSPORT
Function / homology
Function and homology information


Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / Mitochondrial protein degradation / mitochondrial large ribosomal subunit binding / gliogenesis / neural precursor cell proliferation ...Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / Mitochondrial protein degradation / mitochondrial large ribosomal subunit binding / gliogenesis / neural precursor cell proliferation / cardiac muscle tissue development / [2Fe-2S] cluster assembly / oxygen sensor activity / cellular respiration / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / negative regulation of intrinsic apoptotic signaling pathway / ATP synthesis coupled electron transport / quinone binding / : / ATP metabolic process / response to cAMP / aerobic respiration / respiratory electron transport chain / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / electron transport chain / regulation of protein phosphorylation / brain development / negative regulation of cell growth / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / positive regulation of fibroblast proliferation / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / nuclear body / ubiquitin protein ligase binding / mitochondrion / nucleoplasm / 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 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / Acyl carrier protein / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
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 13, 2021-
Header (metadata) releaseNov 23, 2022-
Map releaseNov 23, 2022-
UpdateJun 7, 2023-
Current statusJun 7, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32188.png

Downloads & links

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Map

FileDownload / File: emd_32188.map.gz / Format: CCP4 / Size: 137.1 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 330 pix.
= 354.486 Å		1.07 Å/pix.
x 330 pix.
= 354.486 Å		1.07 Å/pix.
x 330 pix.
= 354.486 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: 0.0236
Minimum - Maximum-0.083130464 - 0.22952995
Average (Standard dev.)0.0002029601 (±0.0039076046)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions330330330
Spacing330330330
CellA=B=C: 354.48602 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] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • 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] flavoprotein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, 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] 1 alpha subcomplex subunit 13
  • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
  • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
  • Protein or peptide: Complex I-20kD
  • Protein or peptide: Acyl carrier protein, mitochondrial
  • Protein or peptide: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, 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 6, mitochondrial
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • 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: #4-#5, #7-#8, #10-#11, #15-#16, #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
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 50.052129 KDa
SequenceString: MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SGYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGAWFASFGR ERNSGTKLFN ISGHVNHPCT VEEEMSVPLK ELIEKHAGGV IGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALVQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV KGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEERMQQFAL QHQ

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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: 23.893281 KDa
SequenceString: MRCLSTPMLL RALAQAQAAH AGHPSARTLH SSAVAATYKF VNMREPSMDM KSVTDRAAQT LLWTELVRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAVCPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV ...String:
MRCLSTPMLL RALAQAQAAH AGHPSARTLH SSAVAATYKF VNMREPSMDM KSVTDRAAQT LLWTELVRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAVCPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV EGPNFEFSTE THEELLYNKE KLLNNGDKWE AEIAANIQAD YLYR

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Macromolecule #3: Complex I-20kD

MacromoleculeName: Complex I-20kD / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: pig (pig)
Molecular weightTheoretical: 21.79534 KDa
SequenceString: MGAAVQVRFV HPSAATDSPS SQPAVSQAGA VVSKPTTLPS SRGEYVVAKL DDLVNWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRF GVVFRASPRQ SDVMIVAGTL TNKMAPALRK VYDQMPEPRY VVSMGSCANG GGYYHYSYSV VRGCDRIVPV D IYVPGCPP ...String:
MGAAVQVRFV HPSAATDSPS SQPAVSQAGA VVSKPTTLPS SRGEYVVAKL DDLVNWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRF GVVFRASPRQ SDVMIVAGTL TNKMAPALRK VYDQMPEPRY VVSMGSCANG GGYYHYSYSV VRGCDRIVPV D IYVPGCPP TAEALLYGIL QLQRKIKREK RLRIWYRR

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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: 14.953313 KDa
SequenceString:
MAASGLPRAA AAAGTSVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHLF QLDISVKQGR DKVREMFMKN AHVTDPRVVD LLVIKGKME LEETINVWKQ RTHIMRFFHE TEAPRPTDFL SKFYVGHDP

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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: 11.099798 KDa
SequenceString:
MAAAAASRGI RAKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD VQPKLWARYA FGQEKNVSLN NFSADQVTR TLENVLSGKA

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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: 17.308186 KDa
SequenceString:
MAARVLCACV RRLPAAFAPL PRIPTVVAAR PLSTTLFPTG AQARSRALQP ALVLAQAPGG VTQLCRRYSD APPLTLEAIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

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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: 13.32159 KDa
SequenceString:
MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGQIPK NAAYRKYTEQ ITNEKLGMVK AEPDVKKLEE QLQGGQIEEV ILQAENELS LARKMLRWKP WEPLVEEPPA NQWKWPI

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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: 12.64859 KDa
SequenceString:
MASATRVIQL LRNWASGRDL QAKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR REAMPPSIVM SSQKVLASGK PAESSAVAE TEKKAVTPAP PIKRWELSKD QPYL

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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: 42.493168 KDa
SequenceString: MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS ...String:
MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS HLNADIKSPS RYLRSKAVGE KEVRAAFPEA TIIKPSDIFG REDRFLNYFA SMRWFGGVPL ISLGKETVKQ PV YIVDVSK GIINAIKDPD AKGKTFAFVG PNRYLLFDLV QYIFAVAYRP FLPYPLPHFA YRWVGRLFEV SPFEPWTTRD KVE RVHMSD MTLPHLPGLE DLGIQATPLE LKAIEVLRRH RTYRWLTSEM EDVKPAKTVN

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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: 12.1728 KDa
SequenceString:
MAASLLLRQG RARALKTVLL EGGVFRGLAP AVSLSAESGR NEKERPPNPK KQSPPKKPTP AAAAAEPFDN STYRNLQHHE YSTYTFLDL NVELSKFRMP QPSSGRQSPR H

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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: 19.746514 KDa
SequenceString:
MAAVSMSVAL KQALWGRRAA AVGAVSVSKV PTRLLSTSTW RLAQDQTQDT QLIAVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWSSTAD PLSNLVLTFS TKEDAVAFAE KNGWSFDVEE RKVPKPKSKS Y GANFSWNK RTRVSTK

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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: 78.670328 KDa
SequenceString: MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNIIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTQPMI RNEKGLLTYT TWE DALSRV AGMLQSFQGN DVAAIAGGLV DAEALVALKD LLNRVDSDSL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVI LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGNHPFSQI LKEAKKPMVV LGSSA LQRS DGTAILAAVS NIAQNIRLSS GVTGDWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKV LFLLGADGGC ITRQDL PKD CFIIYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGMT LPYDTLD QV RSRLEEVSPN LVRYDDVEGA NYFQQANELS KLVNQQLLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGI

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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: 17.162439 KDa
SequenceString:
MELVQVLRRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG RDTFWDVDGS MVPPEWHRW LHCMTDDPPT TKPPTARKYI WTNHKFNVSG TPQQYVPYST TRKKIQEWVP PSTPYK

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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: 27.439533 KDa
SequenceString: MFLTAALRAR ATGFTAQWGR HVRNLHKTAV QNGAGGALFV HRDTPENNPD TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL ...String:
MFLTAALRAR ATGFTAQWGR HVRNLHKTAV QNGAGGALFV HRDTPENNPD TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL FTLIEVECLG ACVNAPMVQI NDNYYEDLTP KDIEEIIDEL KAGKIPKPGP RSGRFSCEPA GGLTSLTEPP KG PGFGVQA GL

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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: 30.241416 KDa
SequenceString: MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS RIRVKTYTDE LTPIESSVTV Y KAANWYER ...String:
MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS RIRVKTYTDE LTPIESSVTV Y KAANWYER EIWDMFGVFF ANHPDLRRIL TDYGFEGHPF RKDFPLSGYV ELRYDDEVKR VVAEPVELAQ EFRKFDLNSP WE AFPAYRQ PPEDLKLEAG DKKPETK

+
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: 53.735777 KDa
SequenceString: MVPVSLWRGK MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSN LTLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMC NE QAYSLAVEKL ...String:
MVPVSLWRGK MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSN LTLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMC NE QAYSLAVEKL LNIQPPPRAQ WIRVLFGEIT RLLNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAY I RPGGVHQDLP LGLLDDIYEF SKNFSFRIDE LEEMLTNNRI WRNRTVDIGV VTAEDALNYG FSGVMLRGSG IQWDLRKTQ PYDVYDQVEF DVPIGSRGDC YDRYLCRVEE MRQSLRIISQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGA TYTAIEAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEVDR

+
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: 13.34895 KDa
SequenceString:
MAAVTFLRLL GRSGAGARNL LGGSRCFGVR TSPTGEKVTH TGQAYDDGDY RRVRFSDRQK EVNENFAIDL IAEQPVSEVG SRVISCDGG GGALGHPRVY INLDKETKTG TCGYCGLQFR QPHH

+
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: 16.911611 KDa
SequenceString:
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMFAVGI GTLLFGYWSM MKWNRERRRL QIEDFEARIA LMPLFQAEKD RRVLQMLRE NLEEEAIIMK DVPDWKVGES VFHTTRWVTP MMGELYGLRT NEEILSATYG FIWYT

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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

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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

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Macromolecule #21: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 21 / 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 #22: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,...

MacromoleculeName: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
type: ligand / ID: 22 / Number of copies: 1 / Formula: PLX
Molecular weightTheoretical: 767.132 Da
Chemical component information

ChemComp-PLX:
(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL / phospholipid*YM

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Macromolecule #23: 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: 23 / 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 #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: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 25 / 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 #26: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 26 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #27: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 27 / Number of copies: 1 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #28: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 28 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 7.5
VitrificationCryogen name: ETHANE

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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: 193234
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: RANDOM ASSIGNMENT

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