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- EMDB-35354: Respiratory complex Membrane domain of CI, focus-refined of type ... -

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Basic information

Entry
Database: EMDB / ID: EMD-35354
TitleRespiratory complex Membrane domain of CI, focus-refined of type I, PERK -/- mouse under cold temperature
Map dataFocus-refined map, PERK -/-, Membrane Domain, Cold Acclimated, Type I of Respiratory Supercomplex
Sample
  • Complex: Respiratory Supercomplex CI:CIII2
    • Protein or peptide: x 24 types
  • Ligand: x 5 types
KeywordsRespiratory complex / Respiratory supercomplex / ELECTRON TRANSPORT
Function / homology
Function and homology information


Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction ...Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / Respiratory electron transport / cellular response to oxygen levels / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / positive regulation of mitochondrial membrane potential / : / ubiquinone binding / iron-sulfur cluster assembly / positive regulation of ATP biosynthetic process / NADH:ubiquinone reductase (H+-translocating) / proton motive force-driven mitochondrial ATP synthesis / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / respiratory chain complex I / : / 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 / ATP synthesis coupled electron transport / quinone binding / negative regulation of reactive oxygen species biosynthetic process / ionotropic glutamate receptor binding / Neutrophil degranulation / aerobic respiration / neurogenesis / cerebellum development / reactive oxygen species metabolic process / response to cocaine / response to nicotine / electron transport chain / response to hydrogen peroxide / mitochondrial intermembrane space / NAD binding / myelin sheath / 4 iron, 4 sulfur cluster binding / in utero embryonic development / response to ethanol / response to oxidative stress / mitochondrial inner membrane / response to hypoxia / nuclear speck / mitochondrial matrix / ubiquitin protein ligase binding / protein-containing complex binding / protein kinase binding / endoplasmic reticulum / mitochondrion / nucleoplasm / metal ion binding / cytoplasm
Similarity search - Function
NADH:ubiquinone oxidoreductase, subunit NDUFB4 / : / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 / MNLL subunit / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / Tim17/Tim22/Tim23/Pmp24 family ...NADH:ubiquinone oxidoreductase, subunit NDUFB4 / : / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 / MNLL subunit / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / Tim17/Tim22/Tim23/Pmp24 family / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, metazoa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, animal type / NADH dehydrogenase 1 beta subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 subunit C2, NDUC2 / NADH-ubiquinone oxidoreductase subunit b14.5b (NDUFC2) / NADH dehydrogenase 1, beta subcomplex, subunit 6 / NADH:ubiquinone oxidoreductase, NDUFB6/B17 subunit / : / NADH:ubiquinone oxidoreductase chain 4, N-terminal / NADH:ubiquinone oxidoreductase, chain 2 / NADH dehydrogenase subunit 2, C-terminal / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / : / NADH-ubiquinone oxidoreductase chain 4, amino terminus / NADH dehydrogenase subunit 2 C-terminus / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase subunit 5, C-terminal / NADH dehydrogenase subunit 5 C-terminus / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NDUFB9, LYR domain / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / Deoxynucleoside kinase domain / Deoxynucleoside kinase / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-quinone oxidoreductase, chain M/4 / NADH-ubiquinone oxidoreductase chain 4L/K / Complex 1 LYR protein domain / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / Complex 1 protein (LYR family) / NAD(P)H-quinone oxidoreductase subunit D/H / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / CHCH / CHCH domain / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / [NiFe]-hydrogenase, large subunit / Acyl carrier protein (ACP) / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial ...NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / Acyl carrier protein, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsShin Y-C / Liao M
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)RO1 DK081418 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)RO1 DK089883 United States
CitationJournal: Cell / Year: 2024
Title: Structural basis of respiratory complex adaptation to cold temperatures.
Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / ...Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / Maofu Liao / Pere Puigserver /
Abstract: In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold ...In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold exposure remains elusive. Herein, we combined thermoregulatory physiology and cryoelectron microscopy (cryo-EM) to study endogenous respiratory supercomplexes from mice exposed to different temperatures. A cold-induced conformation of CI:III (termed type 2) supercomplex was identified with a ∼25° rotation of CIII around its inter-dimer axis, shortening inter-complex Q exchange space, and exhibiting catalytic states that favor electron transfer. Large-scale supercomplex simulations in mitochondrial membranes reveal how lipid-protein arrangements stabilize type 2 complexes to enhance catalytic activity. Together, our cryo-EM studies, multiscale simulations, and biochemical analyses unveil the thermoregulatory mechanisms and dynamics of increased respiratory capacity in brown fat at the structural and energetic level.
History
DepositionFeb 10, 2023-
Header (metadata) releaseSep 18, 2024-
Map releaseSep 18, 2024-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35354.png

Downloads & links

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Map

FileDownload / File: emd_35354.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocus-refined map, PERK -/-, Membrane Domain, Cold Acclimated, Type I of Respiratory Supercomplex
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å

Surface

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.45
Minimum - Maximum-1.1637137 - 2.1474142
Average (Standard dev.)0.005260673 (±0.0753962)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 424.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_35354_msk_1.map
Projections & Slices
AxesZYX

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Half map: Focus-refined map, PERK -/-, Membrane Domain, Cold Acclimated,...

Fileemd_35354_half_map_1.map
AnnotationFocus-refined map, PERK -/-, Membrane Domain, Cold Acclimated, Type I of Respiratory Supercomplex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Focus-refined map, PERK -/-, Membrane Domain, Cold Acclimated,...

Fileemd_35354_half_map_2.map
AnnotationFocus-refined map, PERK -/-, Membrane Domain, Cold Acclimated, Type I of Respiratory Supercomplex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Respiratory Supercomplex CI:CIII2

EntireName: Respiratory Supercomplex CI:CIII2
Components
  • Complex: Respiratory Supercomplex CI:CIII2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4L
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 5
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
    • Protein or peptide: Acyl carrier protein, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: CARDIOLIPIN
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate

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Supramolecule #1: Respiratory Supercomplex CI:CIII2

SupramoleculeName: Respiratory Supercomplex CI:CIII2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#24
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 1.32 MDa

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Macromolecule #1: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 52.693559 KDa
SequenceString: MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVEKLL N IQPPPRAQ ...String:
MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVEKLL N IQPPPRAQ WIRVLFGEIT RILNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAYIR PGGVHQDLPL GL LDDIYEF SKNFSLRIDE VEEMLTNNRI WRNRTVDIGV VTAEDALNYG FSGVMLRGSG IQWDLRKTQP YDVYDQVEFD VPI GSRGDC YDRYLCRVEE MRQSLRIIEQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGAT YTAI EAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEIDR

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

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Macromolecule #2: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 18.62809 KDa
SequenceString:
MNNYIFVLSS LFLVGCLGLA LKPSPIYGGL GLIVSGFVGC LMVLGFGGSF LGLMVFLIYL GGMLVVFGYT TAMATEEYPE TWGSNWLIL GFLVLGVIME VFLICVLNYY DEVGVINLDG LGDWLMYEVD DVGVMLEGGI GVAAMYSCAT WMMVVAGWSL F AGIFIIIE ITRD

UniProtKB: NADH-ubiquinone oxidoreductase chain 6

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Macromolecule #3: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.609619 KDa
SequenceString:
MPSTFFNLTM AFSLSLLGTL MFRSHLMSTL LCLEGMVLSL FIMTSVTSLN SNSMSSMPIP ITILVFAACE AAVGLALLVK VSNTYGTDY VQNLNLLQC

UniProtKB: NADH-ubiquinone oxidoreductase chain 4L

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Macromolecule #4: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 68.519289 KDa
SequenceString: MNIFTTSILL IFILLLSPIL ISMSNLIKHI NFPLYTTTSI KFSFIISLLP LLMFFHNNME YMITTWHWVT MNSMELKMSF KTDFFSILF TSVALFVTWS IMQFSSWYMH SDPNINRFIK YLTLFLITML ILTSANNMFQ LFIGWEGVGI MSFLLIGWWY G RTDANTAA ...String:
MNIFTTSILL IFILLLSPIL ISMSNLIKHI NFPLYTTTSI KFSFIISLLP LLMFFHNNME YMITTWHWVT MNSMELKMSF KTDFFSILF TSVALFVTWS IMQFSSWYMH SDPNINRFIK YLTLFLITML ILTSANNMFQ LFIGWEGVGI MSFLLIGWWY G RTDANTAA LQAILYNRIG DIGFILAMVW FSLNMNSWEL QQIMFSNNND NLIPLMGLLI AATGKSAQFG LHPWLPSAME GP TPVSALL HSSTMVVAGI FLLVRFHPLT TNNNFILTTM LCLGALTTLF TAICALTQND IKKIIAFSTS SQLGLMMVTL GMN QPHLAF LHICTHAFFK AMLFMCSGSI IHSLADEQDI RKMGNITKIM PFTSSCLVIG SLALTGMPFL TGFYSKDLII EAIN TCNTN AWALLITLIA TSMTAMYSMR IIYFVTMTKP RFPPLISINE NDPDLMNPIK RLAFGSIFAG FVISYNIPPT SIPVL TMPW FLKTTALIIS VLGFLIALEL NNLTMKLSMN KANPYSSFST LLGFFPSIIH RITPMKSLNL SLKTSLTLLD LIWLEK TIP KSTSTLHTNM TTLTTNQKGL IKLYFMSFLI NIILIIILYS INLE

UniProtKB: NADH-ubiquinone oxidoreductase chain 5

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Macromolecule #5: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 51.915535 KDa
SequenceString: MLKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLMLMAS QNHLKKDNN VLQKLYISML ISLQILLIMT FSATELIMFY ILFEATLIPT LIIITRWGNQ TERLNAGIYF LFYTLIGSIP L LIALILIQ ...String:
MLKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLMLMAS QNHLKKDNN VLQKLYISML ISLQILLIMT FSATELIMFY ILFEATLIPT LIIITRWGNQ TERLNAGIYF LFYTLIGSIP L LIALILIQ NHVGTLNLMI LSFTTHTLDA SWSNNLLWLA CMMAFLIKMP LYGVHLWLPK AHVEAPIAGS MILAAILLKL GS YGMIRIS IILDPLTKYM AYPFILLSLW GMIMTSSICL RQTDLKSLIA YSSVSHMALV IASIMIQTPW SFMGATMLMI AHG LTSSLL FCLANSNYER IHSRTMIMAR GLQMVFPLMA TWWLMASLAN LALPPSINLM GELFITMSLF SWSNFTIILM GINI IITGM YSMYMIITTQ RGKLTNHMIN LQPSHTRELT LMALHMIPLI LLTTSPKLIT GLTM

UniProtKB: NADH-ubiquinone oxidoreductase chain 4

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Macromolecule #6: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 38.772219 KDa
SequenceString: MNPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF VTQATASMII LLAIVLNYKQ LGTWMFQQQ TNGLILNMTL MALSMKLGLA PFHFWLPEVT QGIPLHMGLI LLTWQKIAPL SILIQIYPLL NSTIILMLAI T SIFMGAWG ...String:
MNPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF VTQATASMII LLAIVLNYKQ LGTWMFQQQ TNGLILNMTL MALSMKLGLA PFHFWLPEVT QGIPLHMGLI LLTWQKIAPL SILIQIYPLL NSTIILMLAI T SIFMGAWG GLNQTQMRKI MAYSSIAHMG WMLAILPYNP SLTLLNLMIY IILTAPMFMA LMLNNSMTIN SISLLWNKTP AM LTMISLM LLSLGGLPPL TGFLPKWIII TELMKNNCLI MATLMAMMAL LNLFFYTRLI YSTSLTMFPT NNNSKMMTHQ TKT KPNLMF STLAIMSTMT LPLAPQLIT

UniProtKB: NADH-ubiquinone oxidoreductase chain 2

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Macromolecule #7: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 40.657375 KDa
SequenceString: MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT KKLHEYSRVI TVDGNICSGK NKLAKEIAQQ LGMKHYPEA GIQYSSTTTG DGRPLDIEFS GSCSLEKFYD DPKSNDGNSY RLQSWLYASR LLQYADALEH LLSTGQGVVL E RSIYSDFV ...String:
MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT KKLHEYSRVI TVDGNICSGK NKLAKEIAQQ LGMKHYPEA GIQYSSTTTG DGRPLDIEFS GSCSLEKFYD DPKSNDGNSY RLQSWLYASR LLQYADALEH LLSTGQGVVL E RSIYSDFV FLEAMYNQGY IRKQCVDHYN EIKRLTLPEY LPPHAVIYID VPVPEVQSRI QKKGDPHEMK VTSAYLQDIE NA YKKTFLP KMSEMCEVLV YDSWEAEDPT KVVEDIEYLK YNKGPWLKQD DWTFHYLRML VQDKTEVLNY TTIPVYLPEI TIG AHQGSR IYNSFRELPG RKYAPGYNAE VGDKWIWLK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial

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Macromolecule #8: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 17.390289 KDa
SequenceString:
MASRVLCACV RRLPAAFAPL PRLPTLALAR PLSTTLCPEG IRRRPGALQS ALALAQVPGT VTHLCRQYSD APPLTLDGIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

UniProtKB: Acyl carrier protein, mitochondrial

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Macromolecule #9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 20.025127 KDa
SequenceString:
MPGIVELPTL EELKVEEVKV SSAVLKAAAH HYGAQCDKTN KEFMLCRWEE KDPRRCLKEG KLVNGCALNF FRQIKSHCAE PFTEYWTCL DYSNMQLFRH CRQQQAKFDQ CVLDKLGWVR PDLGQLSKVT KVKTDRPLPE NPYHSRARPE PNPVIEGDLK P AKHGTRFF FWTV

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

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Macromolecule #10: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 15.130416 KDa
SequenceString:
MAMVKRFFES YHEVPDGTQC HRKTYITTAL GGICGIIGSA YSVSLNPADS TLEAVARVGR YTFTAAAIGA MFGLTTCVSA QVREKPDDP LNYFIGGCAG GLTLGARTHS YGTAAMGCVY MGTAAALFKI GKLEGWELFP TPKV

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

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Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 8.636023 KDa
SequenceString:
MAPSVVLRSF SRLLAPARLP SCSSTRSKFY VREPVNAKPN WLAVGLSVGA SVFMWIYLIQ THNEDVLEYK RRNGLE

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

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Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 subunit C2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C2 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 14.185692 KDa
SequenceString:
MMNGRPGHEP LKFLPDEARS LPPPKLNDPR LVYMGLLGYC TGLMDNMLRM RPVMRAGLHR QLLFVTSFVF AGYFYLKRQN YLYAVKDHD MFGYIKLHPE DFPEKEKKTY AEILEPFHPV R

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C2

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Macromolecule #13: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 12.675772 KDa
SequenceString:
MPFLDIQKKL GISLDRHFMF LSAEQPYKNA ARCHAFEKEW IECAHGIGGT RAKKECKIEF DDFEECLLRY KTMRRMHDIK KQREKLMKE GKYTPPPHHS GREEPRP

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

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Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 6.965109 KDa
SequenceString:
MTLFQLLREH WVHILVPAGF VFGCYLDRKD DEKLTAFRNK SMLFQRELRP NEEVTWK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1

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Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 17.463727 KDa
SequenceString:
MAARLLSLYG RCLSAAGAMR GLPAARVRWE SSRAVIAPSG VEKKRQREPT MQWQEDPEPE DENVYAKNPD FHGYDSDPVV DVWNMRAVF FFGFSIVLVF GTTFVAYVPD YRMQEWARRE AERLVKYREV NGLPIMESNY FDPSKIQLPE DD

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial

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Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 21.742197 KDa
SequenceString:
MAAMSLLQRA SVSALTALSC RRAGPRLGVG SFLTRSFPKT VAPVRHSGDH GKRLFVVKPS LYYDARFLRL MKFYLMLTGI PVIIGITLV NIFIGEAELA EIPEGYIPEH WEYYKHPISR WIARNFYDGP EKNYEKTLAI LQIESEKAEL RLKEQEVRRL M RARGDGPW YQFPTPEKEF IDHSPKATPD N

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial

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Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 15.540085 KDa
SequenceString:
MSGYTPDEKL RLQQLRELRR RWLKDQELSP REPVLPPRRM WPLERFWDNF LRDGAVWKNM VFKAYRSSLF AVSHVLIPMW FVHYYVKYH MATKPYTIVS SKPRIFPGDT ILETGEVIPP MRDFPDQHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

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Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.982437 KDa
SequenceString:
MSALTRLVPF GRVGGRLLRG CRARAAGDSG VRHAGGGVHI QPRYREFPQL TRSQVIQGEF LSSLMWFWIL WRFWHDSDAV LGHFSYPDP SQWTDEELGI PPDDED

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial

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Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.71424 KDa
SequenceString:
MAAGHGHEHG HEHGHGHGKM ELPDYRQWKI EGTPLETVQK KLAARGLRDP WARNEAWRYM GGFAGNITFP SVILKGFKWG FAAFVVALG AEYFLDSQNG DKKHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

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Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 21.903828 KDa
SequenceString:
MAAARAAALG VRWLQRTTRG VVPLEARRAF HMTKDMLPGS YPRTPEERAA AAKKYNMRVE DYEPYPDDGM GYGDYPMLPN RSQHERDPW YQWDHSELRM NWGEPIHWDL DMYIRNRVDT SPTPVSWDVM CKHLFGFVAF MVFMFWVGHV FPSYQPVGPK Q YPYNNLYL ERGGDPTKEP EPVVHYDI

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial

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Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 15.105287 KDa
SequenceString:
MSGSKYKPAP LATLPSTLDP AEYDVSPETR RAQVERLSIR ARLKREYLLQ YNDPKRVSHI EDPALIRWTY ARSANIYPNF RPTPKNSLL GAVAGFGPLI FWYYVFKTDR DRKERLIQEG KLDRKFNISY

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

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Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 22.020123 KDa
SequenceString:
MAFCAPPAYL THQQKVLRLY KRALRHLESW CIHRDKYRYF ACLMRARFEE HKNEKDMMRA TQLLREAEEE FWQNQHPQPY IFPDSPGGT SFERYECYKV PEWCLDYWHP SEKAMYPDYF SKREQWKKLR MESWDREVKQ LQEETSPDGI MTEALPPARR E GDLPPLWW HIVTRPRERP T

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

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Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 16.360804 KDa
SequenceString:
MGAHLTRRYL WDASVEPDPE KIPSFPPDLG FPERKERVMV ATQQEMMDAQ LTLQQRDYCA HYLIRLLKCK RDSFPNFLAC KHEQHDWDY CEHLDYVKRM KEFERERRLL QRKKRRALKE ARVAQGQGEG EVGPEVAL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

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Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 21.054832 KDa
SequenceString:
MPDSWDKDVY PEPPSRTPAP SPQTSLPNPI TYLTKAYDLV VDWPVTLVRE FIERQHAKNR TYYYHRQYRR VPDITECKEG DVLCIYEAE MQWRRDFKVD QEIMNIIQER LKACQQREGE NYQQNCAKEL EQFTKVTKAY QDRYLDLGAY YSARKCLAKQ K QRMLEERK AARQEAAA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

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Macromolecule #25: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 25 / Number of copies: 9 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

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Macromolecule #26: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 26 / Number of copies: 5 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #27: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 27 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #28: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 28 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #29: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...

MacromoleculeName: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
type: ligand / ID: 29 / Number of copies: 1 / Formula: EHZ
Molecular weightTheoretical: 584.703 Da
Chemical component information

ChemComp-EHZ:
~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate

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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

Concentration0.33 mg/mL
BufferpH: 8
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: 50.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7ak5

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45095
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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