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Open data
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Basic information
Entry | Database: PDB / ID: 7dgs | ||||||
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Title | Activity optimized supercomplex state3 | ||||||
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![]() | OXIDOREDUCTASE / respiratory / electron transport | ||||||
Function / homology | ![]() 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 / ubiquinone biosynthetic process ...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 / ubiquinone biosynthetic process / Respiratory electron transport / respiratory chain complex IV / cellular response to oxygen levels / respiratory chain complex / mitochondrial large ribosomal subunit binding / gliogenesis / cytochrome-c oxidase / respiratory chain complex III / oxidative phosphorylation / neural precursor cell proliferation / quinol-cytochrome-c reductase / [2Fe-2S] cluster assembly / mitochondrial electron transport, cytochrome c to oxygen / oxygen sensor activity / Neutrophil degranulation / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / mitochondrial ATP synthesis coupled electron transport / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / acyl binding / ubiquinone binding / acyl carrier activity / electron transport coupled proton transport / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase activity / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / response to cAMP / enzyme regulator activity / neurogenesis / reactive oxygen species metabolic process / aerobic respiration / central nervous system development / fatty acid binding / respiratory electron transport chain / electron transport chain / mitochondrial membrane / brain development / metalloendopeptidase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / circadian rhythm / NAD binding / fatty acid biosynthetic process / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / oxidoreductase activity / mitochondrial matrix / copper ion binding / negative regulation of DNA-templated transcription / apoptotic process / heme binding / protein-containing complex binding / mitochondrion / proteolysis / nucleoplasm / metal ion binding / membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.8 Å | ||||||
![]() | Jeon, T.J. / Lee, S.G. / Yoo, S.H. / Ryu, J.H. / Kim, D.S. / Hyun, J.K. / Kim, H.M. / Ryu, S.E. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.5 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 30675MC ![]() 7dgqC ![]() 7dgrC ![]() 7dgzC ![]() 7dh0C ![]() 7dkfC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
+NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules 98F
+NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules 7624513
+Protein , 4 types, 7 molecules AWMmyoz
+NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules BCDEGHI
+NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 12 molecules JKLNOPQRSTUV
+NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules XYZabcdfhge
+NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules ij
+Cytochrome b-c1 complex subunit ... , 9 types, 18 molecules kwlxpA0qA1rA2sB5tA3uB4vB3
+Cytochrome c oxidase subunit ... , 13 types, 13 molecules A9B9B7A7A6B2A4A5B6B8B0B1A8
+Non-polymers , 13 types, 38 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 |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
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: ![]() |
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
EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||
3D reconstruction | Resolution: 7.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24810 / Symmetry type: POINT |