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- EMDB-6776: Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2 -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-6776 | |||||||||
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Title | Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2 | |||||||||
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Function / homology | ![]() Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly / response to D-galactosamine / Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly ...Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly / response to D-galactosamine / Complex III assembly / Complex III assembly / Complex III assembly / Complex III assembly / protein lipoylation / Complex IV assembly / Complex I biogenesis / TP53 Regulates Metabolic Genes / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / response to mercury ion / Respiratory electron transport / subthalamus development / pons development / protein insertion into mitochondrial inner membrane / mitochondrial respirasome assembly / response to cobalamin / cerebellar Purkinje cell layer development / blastocyst hatching / mitochondrial respiratory chain complex III assembly / ubiquinone biosynthetic process / response to alkaloid / pyramidal neuron development / Respiratory electron transport / cellular respiration / respiratory chain complex IV / thalamus development / Mitochondrial protein import / cellular response to oxygen levels / mesenchymal stem cell proliferation / respiratory chain complex / mitochondrial [2Fe-2S] assembly complex / reproductive system development / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / cytochrome-c oxidase / mesenchymal stem cell differentiation / circulatory system development / regulation of protein phosphorylation / respiratory chain complex III / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / negative regulation of non-canonical NF-kappaB signal transduction / oxidative phosphorylation / cardiac muscle tissue development / quinol-cytochrome-c reductase / neural precursor cell proliferation / response to glucagon / mitochondrial electron transport, cytochrome c to oxygen / positive regulation of mitochondrial membrane potential / [2Fe-2S] cluster assembly / oxygen sensor activity / quinol-cytochrome-c reductase activity / azurophil granule membrane / cytochrome-c oxidase activity / stem cell division / response to copper ion / sodium ion transport / NADH dehydrogenase activity / mitochondrial electron transport, ubiquinol to cytochrome c / iron-sulfur cluster assembly / Mitochondrial protein degradation / hypothalamus development / acyl binding / mitochondrial ATP synthesis coupled electron transport / midbrain development / ubiquinone binding / acyl carrier activity / electron transport coupled proton transport / NADH:ubiquinone reductase (H+-translocating) / positive regulation of ATP biosynthetic process / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / RHOG GTPase cycle / positive regulation of execution phase of apoptosis / respiratory chain complex I / animal organ regeneration / response to hyperoxia / response to cAMP / NADH dehydrogenase (ubiquinone) activity / endopeptidase activator activity / response to cadmium ion / quinone binding / cellular response to interferon-beta / ATP synthesis coupled electron transport / extrinsic apoptotic signaling pathway / negative regulation of reactive oxygen species biosynthetic process / enzyme regulator activity / cellular response to retinoic acid / neurogenesis / ionotropic glutamate receptor binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 17.4 Å | |||||||||
![]() | Gu J / Wu M / Yang M | |||||||||
![]() | ![]() Title: Architecture of Human Mitochondrial Respiratory Megacomplex IIIIIV. Authors: Runyu Guo / Shuai Zong / Meng Wu / Jinke Gu / Maojun Yang / ![]() Abstract: The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, ...The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-IIIIIV (MCIIIIIV) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCIIIIIV forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 387.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.7 KB 17.7 KB | Display Display | ![]() |
Images | ![]() | 20.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 309.1 KB | Display | ![]() |
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Full document | ![]() | 308.7 KB | Display | |
Data in XML | ![]() | 7.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xtiMC ![]() 6771C ![]() 6772C ![]() 6773C ![]() 6774C ![]() 6775C ![]() 5xtbC ![]() 5xtcC ![]() 5xtdC ![]() 5xteC ![]() 5xthC 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 | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.083 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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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 : Human respiratory chain megacomplex-I2III2IV2
Entire | Name: Human respiratory chain megacomplex-I2III2IV2 |
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Components |
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-Supramolecule #1: Human respiratory chain megacomplex-I2III2IV2
Supramolecule | Name: Human respiratory chain megacomplex-I2III2IV2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#70 |
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Source (natural) | Organism: ![]() |
Molecular weight | Experimental: 2.9 MDa |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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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: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
CTF correction | Software - Name: CTFFIND (ver. 3.0) |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 17.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 8600 |
Initial angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |
Final angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |