+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-6775 | |||||||||
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Title | Cryo-EM structure of human respiratory supercomplex I1III2IV1 | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information subthalamus development / pons development / positive regulation of peptidase activity / cerebellar Purkinje cell layer development / protein insertion into mitochondrial inner membrane / Complex I biogenesis / blastocyst hatching / pyramidal neuron development / ubiquinone-6 biosynthetic process / response to mercury ion ...subthalamus development / pons development / positive regulation of peptidase activity / cerebellar Purkinje cell layer development / protein insertion into mitochondrial inner membrane / Complex I biogenesis / blastocyst hatching / pyramidal neuron development / ubiquinone-6 biosynthetic process / response to mercury ion / TP53 Regulates Metabolic Genes / respiratory chain complex IV assembly / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / thalamus development / mitochondrial respirasome assembly / Cytoprotection by HMOX1 / cellular response to oxygen levels / respiratory chain complex IV / Respiratory electron transport / iron-sulfur cluster assembly complex / mitochondrial respiratory chain complex III assembly / mitochondrial large ribosomal subunit binding / respiratory gaseous exchange by respiratory system / Mitochondrial protein import / regulation of oxidative phosphorylation / Respiratory electron transport / gliogenesis / mitochondrial respiratory chain complex III / neural precursor cell proliferation / mitochondrial respiratory chain complex IV / [2Fe-2S] cluster assembly / mitochondrial respirasome / cardiac muscle tissue development / NADH dehydrogenase activity / Glyoxylate metabolism and glycine degradation / response to alkaloid / oxygen sensor activity / cellular respiration / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinone binding / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / acyl binding / response to copper ion / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / response to glucagon / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial ribosome / electron transport coupled proton transport / iron-sulfur cluster assembly / mitochondrial ATP synthesis coupled electron transport / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / acyl carrier activity / azurophil granule membrane / mitochondrial translation / hypothalamus development / midbrain development / NADH:ubiquinone reductase (H+-translocating) / sodium ion transport / response to cobalamin / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / RHOG GTPase cycle / NADH dehydrogenase (ubiquinone) activity / quinone binding / response to hyperoxia / ATP synthesis coupled electron transport / cellular response to interferon-beta / animal organ regeneration / negative regulation of intrinsic apoptotic signaling pathway / enzyme regulator activity / response to cadmium ion / respirasome / aerobic respiration / ATP metabolic process / cellular response to retinoic acid / extrinsic apoptotic signaling pathway / response to cAMP / response to organonitrogen compound / ionotropic glutamate receptor binding / substantia nigra development / reactive oxygen species metabolic process / cerebellum development / respiratory electron transport chain / neurogenesis / response to activity / regulation of mitochondrial membrane potential / response to nicotine / synaptic membrane / generation of precursor metabolites and energy / central nervous system development / fatty acid binding / apoptotic signaling pathway Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
Authors | Gu J / Wu M / Yang M | |||||||||
Citation | Journal: Cell / Year: 2017 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 |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_6775.map.gz | 30.3 MB | EMDB map data format | |
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Header (meta data) | emd-6775-v30.xml emd-6775.xml | 17.5 KB 17.5 KB | Display Display | EMDB header |
Images | emd_6775.png | 25.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6775 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6775 | HTTPS FTP |
-Related structure data
Related structure data | 5xthMC 6771C 6772C 6773C 6774C 6776C 5xtbC 5xtcC 5xtdC 5xteC 5xtiC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_6775.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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
-Sample components
-Entire : Human respiratory supercomplex I1III2IV1
Entire | Name: Human respiratory supercomplex I1III2IV1 |
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Components |
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-Supramolecule #1: Human respiratory supercomplex I1III2IV1
Supramolecule | Name: Human respiratory supercomplex I1III2IV1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#68 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Experimental: 1.7 MDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 1.25 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
CTF correction | Software - Name: CTFFIND (ver. 3.0) |
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Initial angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |
Final angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4) |
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 167761 |