+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-30675 | |||||||||
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Title | Activity optimized supercomplex state3 | |||||||||
Map data | ||||||||||
Sample |
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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 / oxidative phosphorylation / cytochrome-c oxidase / 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) / NADH dehydrogenase activity / apoptotic mitochondrial changes / mitochondrial ATP synthesis coupled electron transport / respiratory chain complex I / : / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / electron transport coupled proton transport / 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 / neurogenesis / respiratory electron transport chain / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / central nervous system development / fatty acid binding / mitochondrial membrane / electron transport chain / brain development / regulation of protein phosphorylation / metalloendopeptidase activity / mitochondrial intermembrane space / fatty acid biosynthetic process / 2 iron, 2 sulfur cluster binding / positive regulation of fibroblast proliferation / NAD binding / 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) / Bovine (cattle) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.8 Å | |||||||||
Authors | Jeon TJ / Lee SG / Yoo SH / Ryu JH / Kim DS / Hyun JK / Kim HM / Ryu SE | |||||||||
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
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_30675.map.gz | 12 MB | EMDB map data format | |
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Header (meta data) | emd-30675-v30.xml emd-30675.xml | 79.6 KB 79.6 KB | Display Display | EMDB header |
Images | emd_30675.png | 98.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30675 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30675 | HTTPS FTP |
-Validation report
Summary document | emd_30675_validation.pdf.gz | 340.6 KB | Display | EMDB validaton report |
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Full document | emd_30675_full_validation.pdf.gz | 340.2 KB | Display | |
Data in XML | emd_30675_validation.xml.gz | 6.3 KB | Display | |
Data in CIF | emd_30675_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30675 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30675 | HTTPS FTP |
-Related structure data
Related structure data | 7dgsMC 7dgqC 7dgrC 7dgzC 7dh0C 7dkfC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_30675.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.3973 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
+Entire : supercomplex of electron transport chain complexes
+Supramolecule #1: supercomplex of electron transport chain complexes
+Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #2: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #3: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #4: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #5: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #6: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #7: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #9: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #10: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
+Macromolecule #11: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
+Macromolecule #12: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
+Macromolecule #13: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
+Macromolecule #14: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
+Macromolecule #15: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
+Macromolecule #16: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #18: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
+Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #30: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #31: Acyl carrier protein, mitochondrial
+Macromolecule #32: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...
+Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
+Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...
+Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #41: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
+Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #44: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #45: Cytochrome b-c1 complex subunit 1, mitochondrial
+Macromolecule #46: Cytochrome b-c1 complex subunit 2, mitochondrial
+Macromolecule #47: Cytochrome b
+Macromolecule #48: Cytochrome c1, heme protein, mitochondrial
+Macromolecule #49: Cytochrome b-c1 complex subunit Rieske, mitochondrial
+Macromolecule #50: Cytochrome b-c1 complex subunit 7
+Macromolecule #51: Cytochrome b-c1 complex subunit 8
+Macromolecule #52: Cytochrome b-c1 complex subunit 6, mitochondrial
+Macromolecule #53: Cytochrome b-c1 complex subunit 10
+Macromolecule #54: Cytochrome b-c1 complex subunit 9
+Macromolecule #55: Cytochrome b-c1 complex subunit Rieske, mitochondrial
+Macromolecule #56: Cytochrome c oxidase subunit 1
+Macromolecule #57: Cytochrome c oxidase subunit 2
+Macromolecule #58: Cytochrome c oxidase subunit 3
+Macromolecule #59: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
+Macromolecule #60: Cytochrome c oxidase subunit 5A, mitochondrial
+Macromolecule #61: Cytochrome c oxidase subunit 5B, mitochondrial
+Macromolecule #62: Cytochrome c oxidase subunit 6A2, mitochondrial
+Macromolecule #63: Cytochrome c oxidase subunit 6B1
+Macromolecule #64: Cytochrome c oxidase subunit 6C
+Macromolecule #65: Cytochrome c oxidase subunit 7A1, mitochondrial
+Macromolecule #66: Cytochrome c oxidase subunit 7B, mitochondrial
+Macromolecule #67: Cytochrome c oxidase subunit 7C, mitochondrial
+Macromolecule #68: Cytochrome c oxidase subunit 8B, mitochondrial
+Macromolecule #69: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #70: CARDIOLIPIN
+Macromolecule #71: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #72: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #73: FLAVIN MONONUCLEOTIDE
+Macromolecule #74: IRON/SULFUR CLUSTER
+Macromolecule #75: ZINC ION
+Macromolecule #76: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #77: PROTOPORPHYRIN IX CONTAINING FE
+Macromolecule #78: HEME C
+Macromolecule #79: HEME-A
+Macromolecule #80: COPPER (II) ION
+Macromolecule #81: MAGNESIUM ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | tissue |
-Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 35.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
CTF correction | Software - Name: CTFFIND (ver. 1.4) |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 7.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 24810 |
Initial angle assignment | Type: NOT APPLICABLE / Software - Name: RELION (ver. 2.0) |
Final angle assignment | Type: NOT APPLICABLE / Software - Name: RELION (ver. 2.0) |