+Open data
-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 information Complex III assembly / Complex I biogenesis / Complex IV assembly / Mitochondrial protein import / TP53 Regulates Metabolic Genes / RHOG GTPase cycle / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / respiratory chain complex III ...Complex III assembly / Complex I biogenesis / Complex IV assembly / Mitochondrial protein import / TP53 Regulates Metabolic Genes / RHOG GTPase cycle / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / respiratory chain complex III / respiratory chain complex IV / regulation of oxidative phosphorylation / ubiquinone-6 biosynthetic process / Respiratory electron transport / cellular response to oxygen levels / : / : / : / mitochondrial large ribosomal subunit binding / gliogenesis / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / neural precursor cell proliferation / ubiquinol-cytochrome-c reductase activity / [2Fe-2S] cluster assembly / oxygen sensor activity / mitochondrial electron transport, cytochrome c to oxygen / cellular respiration / Neutrophil degranulation / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / ubiquinone binding / Mitochondrial protein degradation / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / respiratory chain complex I / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / : / enzyme regulator activity / ATP metabolic process / response to cAMP / aerobic respiration / respiratory electron transport chain / reactive oxygen species metabolic process / neurogenesis / regulation of mitochondrial membrane potential / central nervous system development / fatty acid binding / mitochondrial membrane / electron transport chain / regulation of protein phosphorylation / brain development / metalloendopeptidase activity / mitochondrial intermembrane space / fatty acid biosynthetic process / 2 iron, 2 sulfur cluster binding / NAD binding / positive regulation of fibroblast proliferation / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / oxidoreductase activity / mitochondrial matrix / copper ion binding / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / heme binding / protein-containing complex binding / apoptotic process / mitochondrion / proteolysis / nucleoplasm / membrane / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
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: 2022 Title: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-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
Summary document | 7dkf_validation.pdf.gz | 2.4 MB | Display | wwPDB validaton report |
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Full document | 7dkf_full_validation.pdf.gz | 3 MB | Display | |
Data in XML | 7dkf_validation.xml.gz | 406.7 KB | Display | |
Data in CIF | 7dkf_validation.cif.gz | 604.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dk/7dkf ftp://data.pdbj.org/pub/pdb/validation_reports/dk/7dkf | HTTPS FTP |
-Related structure data
Related structure data | 30706MC 7dgqC 7dgrC 7dgsC 7dgzC 7dh0C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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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 |
-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: Bos taurus (cattle) |
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 |
-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) |
-Processing
EM software |
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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 |