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Open data
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Basic information
| Entry | Database: PDB / ID: 9vpc | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the IF1 bound bovine ATP synthase tetramer | |||||||||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / ATP synthase/hydrolase / oligomer / membrane bending / mammalian mitochondria | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / negative regulation of hydrolase activity / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination / proton channel activity ...negative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / negative regulation of hydrolase activity / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination / proton channel activity / heme biosynthetic process / Mitochondrial protein degradation / negative regulation of endothelial cell proliferation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton motive force-driven mitochondrial ATP synthesis / MHC class I protein binding / positive regulation of blood vessel endothelial cell migration / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / aerobic respiration / erythrocyte differentiation / ADP binding / mitochondrial membrane / ATPase binding / protein homotetramerization / calmodulin binding / mitochondrial inner membrane / lipid binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / metal ion binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.2 Å | |||||||||||||||||||||||||||
Authors | Nakano, A. / Jiko, C. / Yamashita, E. / Yokoyama, K. / Gerle, C. | |||||||||||||||||||||||||||
| Funding support | Japan, 2items
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Citation | Journal: Biorxiv / Year: 2025Title: A planar dimer of bovine ATP synthase Authors: Jiko, C. / Nakano, A. / Teshirogi, Y. / Yamashita, E. / Kurisu, G. / Standley, D. / Terada, T. / Mitsuoka, K. / Yokoyama, K. / Gerle, C. | |||||||||||||||||||||||||||
| 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 | 9vpc.cif.gz | 2.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9vpc.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9vpc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vp/9vpc ftp://data.pdbj.org/pub/pdb/validation_reports/vp/9vpc | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 9vpbC ![]() 9vpdC 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
-ATP synthase ... , 17 types, 112 molecules 182838481A1B1C2A2B2C3A3B3C4A4B4C1D1E1F2D2E2F3D3E3F4D4E4F1G2G...
| #1: Protein | Mass: 7944.523 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 59765.469 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 56340.199 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P00829, H+-transporting two-sector ATPase #4: Protein | Mass: 33119.035 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 17626.992 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 5793.889 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 15041.492 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 23351.596 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 24801.785 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 28859.629 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 18719.453 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 8336.688 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 10315.207 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 11429.393 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 12549.321 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 6846.093 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 6443.579 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein , 1 types, 4 molecules 1J2J3J4J
| #7: Protein | Mass: 12326.715 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Details
| Has protein modification | N |
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-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: Bovine F-ATP synthase in the oligomeric form of an IF1 bound tetramer Type: COMPLEX Details: Oligomer fractions of bovine F-ATP synthase obtained from heart muscle tissue mitochondria. Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 2.5 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.3 |
| Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 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: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| 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 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 7.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 39764 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||
| Atomic model building | PDB-ID: 7AJD Accession code: 7AJD / Source name: PDB / Type: experimental model |
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About Yorodumi






Japan, 2items
Citation


PDBj




FIELD EMISSION GUN
