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- EMDB-16517: Cryo-EM structure NDUFS4 knockout complex I from Mus musculus hea... -

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Basic information

Entry
Database: EMDB / ID: EMD-16517
TitleCryo-EM structure NDUFS4 knockout complex I from Mus musculus heart (Class 2 N-domain).
Map dataglobally sharpened focused refinement
Sample
  • Complex: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
  • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
  • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
  • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
  • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FLAVIN MONONUCLEOTIDE
KeywordsNADH ubiquinone oxidoreductase / Complex I / OXIDOREDUCTASE
Function / homology
Function and homology information


Complex I biogenesis / Respiratory electron transport / blastocyst hatching / cardiac muscle tissue development / cellular respiration / mitochondrial ATP synthesis coupled electron transport / NADH:ubiquinone reductase (H+-translocating) / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes ...Complex I biogenesis / Respiratory electron transport / blastocyst hatching / cardiac muscle tissue development / cellular respiration / mitochondrial ATP synthesis coupled electron transport / NADH:ubiquinone reductase (H+-translocating) / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase (ubiquinone) activity / aerobic respiration / ATP metabolic process / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / myelin sheath / nervous system development / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / mitochondrion / metal ion binding / cytosol
Similarity search - Function
NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / 2Fe-2S iron-sulfur cluster binding domain ...NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NuoE domain / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Thioredoxin-like superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.25 Å
AuthorsYin Z / Bridges HR / Agip ANA / Hirst J
Funding support United Kingdom, 3 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_U105663141 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UU_00015/2 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UU_00028/1 United Kingdom
CitationJournal: EMBO J / Year: 2024
Title: Structural insights into respiratory complex I deficiency and assembly from the mitochondrial disease-related ndufs4 mouse.
Authors: Zhan Yin / Ahmed-Noor A Agip / Hannah R Bridges / Judy Hirst /
Abstract: Respiratory complex I (NADH:ubiquinone oxidoreductase) is essential for cellular energy production and NAD homeostasis. Complex I mutations cause neuromuscular, mitochondrial diseases, such as Leigh ...Respiratory complex I (NADH:ubiquinone oxidoreductase) is essential for cellular energy production and NAD homeostasis. Complex I mutations cause neuromuscular, mitochondrial diseases, such as Leigh Syndrome, but their molecular-level consequences remain poorly understood. Here, we use a popular complex I-linked mitochondrial disease model, the ndufs4 mouse, to define the structural, biochemical, and functional consequences of the absence of subunit NDUFS4. Cryo-EM analyses of the complex I from ndufs4 mouse hearts revealed a loose association of the NADH-dehydrogenase module, and discrete classes containing either assembly factor NDUFAF2 or subunit NDUFS6. Subunit NDUFA12, which replaces its paralogue NDUFAF2 in mature complex I, is absent from all classes, compounding the deletion of NDUFS4 and preventing maturation of an NDUFS4-free enzyme. We propose that NDUFAF2 recruits the NADH-dehydrogenase module during assembly of the complex. Taken together, the findings provide new molecular-level understanding of the ndufs4 mouse model and complex I-linked mitochondrial disease.
History
DepositionJan 24, 2023-
Header (metadata) releaseDec 20, 2023-
Map releaseDec 20, 2023-
UpdateJan 31, 2024-
Current statusJan 31, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16517.png

Downloads & links

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Map

FileDownload / File: emd_16517.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationglobally sharpened focused refinement
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.35 Å/pix.
x 450 pix.
= 608.4 Å		1.35 Å/pix.
x 450 pix.
= 608.4 Å		1.35 Å/pix.
x 450 pix.
= 608.4 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.352 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.7
Minimum - Maximum-4.9082985 - 14.807112999999999
Average (Standard dev.)0.0010817844 (±0.3506364)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 608.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_16517_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 1

Fileemd_16517_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_16517_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

EntireName: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Components
  • Complex: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
  • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
  • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
  • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
  • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FLAVIN MONONUCLEOTIDE

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Supramolecule #1: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

SupramoleculeName: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 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: 27.318336 KDa
SequenceString: MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF ...String:
MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTPK DIEEIIDELK AGKVPKPGPR SGRFCCEPAG GLTSLTEPPK GP GFGVQAG L

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

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Macromolecule #2: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
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: 50.904152 KDa
SequenceString: MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SDYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGTWFAGFGR ERNSGTKLFN ISGHVNHPCT VEEEMSVPLK ELIEKHAGGV TGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALVQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV KGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEDRMQRFAQ QHRAWQAAS

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

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Macromolecule #3: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
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: 79.866688 KDa
SequenceString: MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNVIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTEPMV RNEKGLLTYT SWE DALSRV AGMLQNFEGN AVAAIAGGLV DAEALVALKD LLNKVDSDNL CTEEIFPTEG AGTDLRSNYL LNTTIAGVEE ADVV LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGRHSFCEV LKDAKKPMVV LGSSA LQRD DGAAILVAVS NMVQKIRVTT GVAAEWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKM LFLLGADGGC ITRQDL PKD CFIVYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGIT LPYDTLD QV RNRLEEVSPN LVRYDDIEET NYFQQASELA KLVNQEVLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGAQA V EEPSIC

UniProtKB: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

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Macromolecule #4: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.932675 KDa
SequenceString:
MAAAAASRAV GAKLGLREIR VHLCQRSPGS QGVRDFIVQR YVELKKAHPN LPILIRECSE VQPKLWARYA FGQEKTVSLN NLSADEVTR AMQNVLSGKA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

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Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.833504 KDa
SequenceString:
MAVSLLLRGG RIRALKAVLL EARVFPGELV SVVRLSTESE KSAKEKELHP KTQSVLKEPE PTDTTTYKNL QHHDYNTYTF LDLNLDLSK FRLPQPSSGR ESPRH

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

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Macromolecule #6: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 6 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

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Macromolecule #7: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 7 / Number of copies: 3 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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Macromolecule #8: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 8 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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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

Concentration3.82 mg/mL
BufferpH: 7.14
Component:
ConcentrationFormulaName
20.0 mMNH2C(CH2OH)3tris
150.0 mMNaClSodium chloridesodium chloride
0.05 %C24H46O11DDM
2.5 mMC16H19N2NaO14S2BS3

Details: pH was corrected at room temperature ~22 C
GridModel: UltrAuFoil / Material: GOLD / Support film - Material: GOLD / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.9 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 45.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Details: ACADVL is associated with complex I and the startup model used was EMD-11377.
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.25 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 50914
FSC plot (resolution estimation)

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