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Yorodumi- PDB-9w2u: Cryo-EM structure of complex I on the bovine heart submitochondri... -
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Basic information
| Entry | Database: PDB / ID: 9w2u | ||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of complex I on the bovine heart submitochondrial particles, open | ||||||||||||||||||||||||||||||
Components |
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Keywords | OXIDOREDUCTASE / respiratory chain complex / supercomplex / submitochondrial particles / MOTOR PROTEIN | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationComplex I biogenesis / Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Complex I biogenesis / Mitochondrial ribosome-associated quality control / Complex I biogenesis / Respiratory electron transport / Respiratory electron transport ...Complex I biogenesis / Mitochondrial protein import / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Complex I biogenesis / Mitochondrial ribosome-associated quality control / Complex I biogenesis / Respiratory electron transport / Respiratory electron transport / NADH dehydrogenase complex / Respiratory electron transport / protein lipoylation / cellular response to oxygen levels / iron-sulfur cluster assembly complex / ubiquinone biosynthetic process / mitochondrial large ribosomal subunit binding / mitochondrial [2Fe-2S] assembly complex / gliogenesis / Mitochondrial translation termination / Neutrophil degranulation / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / iron-sulfur cluster assembly / Mitochondrial protein degradation / NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / mitochondrial ATP synthesis coupled electron transport / electron transport coupled proton transport / proton motive force-driven mitochondrial ATP synthesis / mitochondrial electron transport, NADH to ubiquinone / acyl binding / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase activity / oxidoreductase activity, acting on NAD(P)H / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / response to cAMP / acyl carrier activity / quinone binding / ATP synthesis coupled electron transport / reactive oxygen species metabolic process / Mitochondrial protein degradation / neurogenesis / aerobic respiration / fatty acid binding / respiratory electron transport chain / electron transport chain / circadian rhythm / brain development / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / mitochondrial membrane / NAD binding / fatty acid biosynthetic process / FMN binding / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / mitochondrial inner membrane / mitochondrial matrix / negative regulation of DNA-templated transcription / apoptotic process / protein-containing complex binding / structural molecule activity / mitochondrion / RNA binding / nucleoplasm / metal ion binding / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | ||||||||||||||||||||||||||||||
Authors | Nakano, A. / Masuya, T. / Akisada, S. / Ishikawa-Fukuda, M. / Mitsuoka, K. / Miyoshi, H. / Murai, M. / Yokoyama, K. | ||||||||||||||||||||||||||||||
| Funding support | Japan, 3items
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Citation | Journal: Nat Commun / Year: 2026Title: Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane. Authors: Atsuki Nakano / Takahiro Masuya / Shinsuke Akisada / Moe Ishikawa-Fukuda / Kaoru Mitsuoka / Hideto Miyoshi / Masatoshi Murai / Ken Yokoyama / ![]() Abstract: Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the ...Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of FF ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most FF complexes were observed as dimers stabilized by the regulatory factor IF₁, and a tetrameric assembly comprising two FF-IF₁ dimers arranged linearly was also identified. This finding indicates that the tetrameric units of FF are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F domain maps resolve the e-subunit- c₈-ring interface and show no discrete density for a tightly bound lipid within the c₈-ring. In addition to the previously reported SCs compositions CI₁CIII₂CIV₁ and CI₁CIII₂CIV₂, our analysis identified an additional assembly with the composition CI₁CIII₂CIV₃, as well as a CI₂CIII₂CIV₆ mega-complex. This approach enables rapid structural determination of FF ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture. | ||||||||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9w2u.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9w2u.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 9w2u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w2/9w2u ftp://data.pdbj.org/pub/pdb/validation_reports/w2/9w2u | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 65580MC ![]() 9w2rC ![]() 9w2sC ![]() 9w2tC ![]() 9w2vC ![]() 9w2xC ![]() 9w2yC ![]() 9w2zC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules JAHKLMN
| #1: Protein | Mass: 19110.488 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P03924, NADH:ubiquinone reductase (H+-translocating) |
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| #2: Protein | Mass: 12927.325 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q8WAB4, NADH:ubiquinone reductase (H+-translocating) |
| #9: Protein | Mass: 35557.574 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P03887, NADH:ubiquinone reductase (H+-translocating) |
| #11: Protein | Mass: 10668.989 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q6EMS3, NADH:ubiquinone reductase (H+-translocating) |
| #12: Protein | Mass: 68196.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P03920, NADH:ubiquinone reductase (H+-translocating) |
| #13: Protein | Mass: 51999.559 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P03910, NADH:ubiquinone reductase (H+-translocating) |
| #14: Protein | Mass: 39143.734 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P03892, NADH:ubiquinone reductase (H+-translocating) |
-NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules BCDIQRe
| #3: Protein | Mass: 17773.889 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P42026, NADH:ubiquinone reductase (H+-translocating) |
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| #4: Protein | Mass: 24547.701 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P23709, NADH:ubiquinone reductase (H+-translocating) |
| #5: Protein | Mass: 49263.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P17694, NADH:ubiquinone reductase (H+-translocating) |
| #10: Protein | Mass: 20219.947 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P42028, NADH:ubiquinone reductase (H+-translocating) |
| #17: Protein | Mass: 14918.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #18: Protein | Mass: 10551.720 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #31: Protein | Mass: 11835.733 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules EFs
| #6: Protein | Mass: 23655.178 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P04394, NADH:ubiquinone reductase (H+-translocating) |
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| #7: Protein | Mass: 47383.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P25708, NADH:ubiquinone reductase (H+-translocating) |
| #45: Protein/peptide | Mass: 5392.883 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 1 types, 1 molecules G
| #8: Protein | Mass: 76628.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P15690, NADH:ubiquinone reductase (H+-translocating) |
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-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 12 molecules OPSVWXtZabqv
| #15: Protein | Mass: 36754.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #16: Protein | Mass: 38932.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #19: Protein | Mass: 9970.458 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #22: Protein | Mass: 13203.414 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #23: Protein | Mass: 13884.140 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #24: Protein | Mass: 19992.936 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #25: Protein | Mass: 14666.862 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #26: Protein | Mass: 16421.041 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #27: Protein | Mass: 8117.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #28: Protein | Mass: 9226.654 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #43: Protein | Mass: 17115.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #44: Protein | Mass: 12590.425 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Acyl carrier protein, ... , 2 types, 2 molecules TU
| #20: Protein | Mass: 9846.298 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #21: Protein | Mass: 9917.375 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules cd
| #29: Protein/peptide | Mass: 5836.698 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #30: Protein | Mass: 13986.099 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules fghujklmnop
| #32: Protein | Mass: 6978.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #33: Protein | Mass: 11897.325 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #34: Protein | Mass: 16297.941 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #35: Protein | Mass: 15444.929 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #36: Protein | Mass: 8385.201 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #37: Protein | Mass: 9229.537 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #38: Protein | Mass: 18599.799 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #39: Protein | Mass: 15075.063 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #40: Protein | Mass: 21134.076 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #41: Protein | Mass: 14978.120 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #42: Protein | Mass: 20701.510 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Non-polymers , 14 types, 57 molecules 


























| #46: Chemical | ChemComp-FME / #47: Chemical | ChemComp-PC1 / #48: Chemical | ChemComp-SF4 / #49: Chemical | #50: Chemical | ChemComp-FMN / | #51: Chemical | ChemComp-K / | #52: Chemical | ChemComp-3PE / #53: Chemical | ChemComp-CDL / #54: Chemical | ChemComp-CHD / | #55: Chemical | ChemComp-GTP / | #56: Chemical | ChemComp-MG / | #57: Chemical | ChemComp-NDP / | #58: Chemical | ChemComp-ZN / | #59: Chemical | ChemComp-MYR / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Complex I on the bovine heart submitochondrial particles Type: COMPLEX / Entity ID: #1-#45 / Source: NATURAL |
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| Molecular weight | Value: 0.60 MDa / Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 30421492 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 252601 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||
| Atomic model building | PDB-ID: 7QSK Accession code: 7QSK / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.6 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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Japan, 3items
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FIELD EMISSION GUN
