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Open data
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Basic information
| Entry | Database: PDB / ID: 7dkf | ||||||||||||||||||
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| Title | Activity optimized supercomplex state4 | ||||||||||||||||||
Components |
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Keywords | OXIDOREDUCTASE / respiratory / electron transport | ||||||||||||||||||
| Function / homology | Function and homology informationComplex III assembly / Complex I biogenesis / Complex IV assembly / TP53 Regulates Metabolic Genes / Mitochondrial protein import / RHOG GTPase cycle / respiratory chain complex IV assembly / subthalamus development / pons development / Cytoprotection by HMOX1 ...Complex III assembly / Complex I biogenesis / Complex IV assembly / TP53 Regulates Metabolic Genes / Mitochondrial protein import / RHOG GTPase cycle / respiratory chain complex IV assembly / subthalamus development / pons development / Cytoprotection by HMOX1 / mitochondrial respirasome assembly / cerebellar Purkinje cell layer development / mitochondrial processing peptidase complex / thalamus development / Respiratory electron transport / pyramidal neuron development / respiratory chain complex IV / mitochondrial ATP synthesis coupled electron transport / cellular response to oxygen levels / respiratory chain complex / mitochondrial large ribosomal subunit binding / ubiquinone biosynthetic process / neural precursor cell proliferation / gliogenesis / Mitochondrial translation termination / cytochrome-c oxidase / respiratory chain complex III / mitochondrial electron transport, cytochrome c to oxygen / quinol-cytochrome-c reductase / oxidative phosphorylation / Neutrophil degranulation / [2Fe-2S] cluster assembly / oxygen sensor activity / quinol-cytochrome-c reductase activity / midbrain development / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / mitochondrial electron transport, NADH to ubiquinone / hypothalamus development / electron transport coupled proton transport / acyl binding / NADH dehydrogenase activity / mitochondrial respiratory chain complex I assembly / reactive oxygen species metabolic process / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / response to cAMP / quinone binding / neurogenesis / ATP synthesis coupled electron transport / enzyme regulator activity / fatty acid binding / hippocampus development / iron-sulfur cluster binding / aerobic respiration / central nervous system development / respiratory electron transport chain / brain development / 2 iron, 2 sulfur cluster binding / circadian rhythm / metalloendopeptidase activity / electron transport chain / mitochondrial intermembrane space / fatty acid biosynthetic process / NAD binding / mitochondrial membrane / FMN binding / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / protein-macromolecule adaptor activity / mitochondrial inner membrane / mitochondrial matrix / copper ion binding / negative regulation of DNA-templated transcription / heme binding / protein-containing complex binding / mitochondrion / proteolysis / metal ion binding / nucleoplasm / membrane / nucleus / cytoplasm Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.3 Å | ||||||||||||||||||
Authors | Jeon, T.J. / Lee, S.G. / Yoo, S.H. / Ryu, J.H. / Kim, D.S. / Hyun, J.K. / Kim, H.M. / Ryu, S.E. | ||||||||||||||||||
Citation | Journal: Antioxid Redox Signal / Year: 2022Title: A Dynamic Substrate Pool Revealed by cryo-EM of a Lipid-Preserved Respiratory Supercomplex. Authors: Tae Jin Jeon / Seong-Gyu Lee / Suk Hyun Yoo / Myeongbin Kim / Dabin Song / Joonghyun Ryu / Hwangseo Park / Deok-Soo Kim / Jaekyung Hyun / Ho Min Kim / Seong Eon Ryu / ![]() Abstract: Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in ... Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in physiologically relevant conditions, we conducted cryoelectron microscopy studies with supercomplexes in a lipid-preserving state. Here, we present cryoelectron microscopy structures of bovine respiratory supercomplex IIIIIV by using a lipid-preserving sample preparation. The preparation greatly enhances the intercomplex quinone transfer activity. The structures reveal large intercomplex motions that result in different shapes and sizes of the intercomplex space between complexes I and III, forming a dynamic substrate pool. Biochemical and structural analyses indicated that intercomplex phospholipids mediate the intercomplex motions. An analysis of the different classes of focus-refined complex I showed that structural switches due to quinone reduction led to the formation of a novel channel that could transfer reduced quinones to the intercomplex substrate pool. Our results indicate potential mechanism for the facilitated electron transfer involving a dynamic substrate pool and intercomplex movement by which supercomplexes play an active role in the regulation of metabolic flux and reactive oxygen species. | ||||||||||||||||||
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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 | 7dkf.cif.gz | 2.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7dkf.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7dkf.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dk/7dkf ftp://data.pdbj.org/pub/pdb/validation_reports/dk/7dkf | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 30706MC ![]() 7dgqC ![]() 7dgrC ![]() 7dgsC ![]() 7dgzC ![]() 7dh0C 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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Components
+Cytochrome b-c1 complex subunit ... , 9 types, 18 molecules A1M1B1N1E1Q1F1R1G1S1H1T1I1U1J1V1K1W1
+Protein , 4 types, 7 molecules C1O1D1P1A2W2M2
+NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules 22324252721262
+NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules 8292F2
+NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules B2C2D2E2G2H2I2
+NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 12 molecules J2K2L2N2O2P2Q2R2S2T2U2V2
+NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules X2Y2Z2a2b2c2d2f2h2g2e2
+NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules i2j2
+Cytochrome c oxidase subunit ... , 13 types, 13 molecules A3B3C3D3E3F3G3H3I3J3K3L3M3
+Non-polymers , 13 types, 31 molecules 
























+Details
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: TISSUE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: supercomplex of electron transport chain complexes / Type: COMPLEX / Entity ID: #1-#68 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 35 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||
| 3D reconstruction | Resolution: 8.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 11651 / Symmetry type: POINT |
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FIELD EMISSION GUN