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Yorodumi- EMDB-9539: Cryo-EM structure of mammalian respiratory supercomplex I1III2IV1 -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-9539 | ||||||||||||
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| Title | Cryo-EM structure of mammalian respiratory supercomplex I1III2IV1 | ||||||||||||
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Keywords | Cryo-EM / Mammalian / Respiratory / Supercomplex / ELECTRON TRANSPORT | ||||||||||||
| Function / homology | Function and homology informationComplex IV assembly / Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / Complex III assembly / Mitochondrial protein import / subthalamus development / pons development / : / cerebellar Purkinje cell layer development / mitochondrial respiratory chain complex III assembly ...Complex IV assembly / Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / Complex III assembly / Mitochondrial protein import / subthalamus development / pons development / : / cerebellar Purkinje cell layer development / mitochondrial respiratory chain complex III assembly / Complex I biogenesis / Respiratory electron transport / pyramidal neuron development / anterograde axonal transport / respiratory chain complex IV / thalamus development / Mitochondrial protein degradation / cellular response to oxygen levels / mesenchymal stem cell proliferation / reproductive system development / gliogenesis / respiratory chain complex III / mesenchymal stem cell differentiation / circulatory system development / mitochondrial electron transport, cytochrome c to oxygen / neural precursor cell proliferation / oxygen sensor activity / quinol-cytochrome-c reductase activity / stem cell division / mitochondrial electron transport, ubiquinol to cytochrome c / hypothalamus development / midbrain development / ubiquinone binding / acyl binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / axon cytoplasm / muscle contraction / reactive oxygen species metabolic process / aerobic respiration / regulation of mitochondrial membrane potential / hippocampus development / DNA damage response, signal transduction by p53 class mediator / kidney development / electron transport chain / fatty acid metabolic process / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / multicellular organism growth / NAD binding / cellular senescence / FMN binding / 4 iron, 4 sulfur cluster binding / gene expression / oxidoreductase activity / mitochondrial inner membrane / nuclear speck / mitochondrial matrix / ubiquitin protein ligase binding / protein-containing complex / mitochondrion / nucleoplasm / metal ion binding / membrane Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | ||||||||||||
Authors | Gu J / Wu M | ||||||||||||
| Funding support | China, 3 items
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Citation | Journal: Cell / Year: 2016Title: Structure of Mammalian Respiratory Supercomplex IIIIIV. Authors: Meng Wu / Jinke Gu / Runyu Guo / Yushen Huang / Maojun Yang / ![]() Abstract: The mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to ...The mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to synthesize ATP. The precise arrangement of SCs is largely unknown. Here, we report a 4.0-Å cryo-electron microscopy (cryo-EM) structure of the major SC in porcine heart, the 1.7-MDa SCIIIIIV. The complex III (CIII) dimer and complex IV (CIV) bind at the same side of the L-shaped complex I (CI). Several accessory or supernumerary subunits of CI, such as NDUFA11, NDUFB4, NDUFB8, and NDUFB9, directly contribute to the oligomerization of CI, CIII, and CIV. COX7C and COX7A of CIV attach CIV to the concave surface formed by CIII and the distal end of membrane arm of CI. The structure suggests a possible mechanism by which electrons are transferred from NADH to cytochrome c and provides a platform for future functional dissection of respiration. | ||||||||||||
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Structure visualization
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
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Downloads & links
-EMDB archive
| Map data | emd_9539.map.gz | 29.6 MB | EMDB map data format | |
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| Header (meta data) | emd-9539-v30.xml emd-9539.xml | 88.3 KB 88.3 KB | Display Display | EMDB header |
| Images | emd_9539.png | 15.6 KB | ||
| Filedesc metadata | emd-9539.cif.gz | 18.1 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-9539 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-9539 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5gupMC ![]() 6718C ![]() 6719C ![]() 6720C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_9539.map.gz / Format: CCP4 / Size: 421.9 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: 1.08 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : Respiratory supercomplex I1III2IV1
+Supramolecule #1: Respiratory supercomplex I1III2IV1
+Macromolecule #1: Cytochrome c oxidase subunit 6C
+Macromolecule #2: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
+Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
+Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #6: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #7: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
+Macromolecule #8: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
+Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
+Macromolecule #10: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...
+Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
+Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
+Macromolecule #15: Acyl carrier protein, mitochondrial
+Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
+Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #30: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
+Macromolecule #31: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #32: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #33: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #34: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #35: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #36: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #37: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #41: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #42: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #44: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+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 7
+Macromolecule #50: Cytochrome b-c1 complex subunit 8
+Macromolecule #51: Cytochrome b-c1 complex subunit 6, mitochondrial
+Macromolecule #52: Cytochrome b-c1 complex subunit 9
+Macromolecule #53: Cytochrome b-c1 complex subunit Rieske, mitochondrial
+Macromolecule #54: Cytochrome b-c1 complex subunit 10
+Macromolecule #55: Cytochrome b-c1 complex subunit Rieske transit peptide, mitochondrial
+Macromolecule #56: Cytochrome c oxidase subunit 8B, mitochondrial
+Macromolecule #57: Cytochrome c oxidase subunit 7A1, mitochondrial
+Macromolecule #58: Cytochrome c oxidase subunit 7B, mitochondrial
+Macromolecule #59: Cytochrome c oxidase subunit 7C, mitochondrial
+Macromolecule #60: Cytochrome c oxidase subunit 1
+Macromolecule #61: Cytochrome c oxidase subunit 2
+Macromolecule #62: Cytochrome c oxidase subunit 3
+Macromolecule #63: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
+Macromolecule #64: Cytochrome c oxidase subunit 5A, mitochondrial
+Macromolecule #65: Cytochrome c oxidase subunit 5B, mitochondrial
+Macromolecule #66: Cytochrome c oxidase subunit 6A, mitochondrial
+Macromolecule #67: Cytochrome c oxidase subunit 6B1
+Macromolecule #68: IRON/SULFUR CLUSTER
+Macromolecule #69: FLAVIN MONONUCLEOTIDE
+Macromolecule #70: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #71: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,...
+Macromolecule #72: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #73: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #74: CARDIOLIPIN
+Macromolecule #75: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
+Macromolecule #76: PROTOPORPHYRIN IX CONTAINING FE
+Macromolecule #77: HEME C
+Macromolecule #78: HEME-A
+Macromolecule #79: COPPER (II) ION
+Macromolecule #80: MAGNESIUM ION
+Macromolecule #81: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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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: 1.25 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: OTHER |
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| Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 161912 |
| Initial angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |
| Final angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |
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Keywords
Authors
China, 3 items
Citation
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