+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-6773 | |||||||||
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Title | Cryo-EM structure of human respiratory complex I | |||||||||
Map data | This map was obtained by sub-region refinement. | |||||||||
Sample |
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Function / homology | Function and homology information positive regulation of peptidase activity / protein insertion into mitochondrial inner membrane / Complex I biogenesis / response to light intensity / blastocyst hatching / ubiquinone-6 biosynthetic process / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / cellular response to oxygen levels / Respiratory electron transport ...positive regulation of peptidase activity / protein insertion into mitochondrial inner membrane / Complex I biogenesis / response to light intensity / blastocyst hatching / ubiquinone-6 biosynthetic process / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / cellular response to oxygen levels / Respiratory electron transport / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / respiratory gaseous exchange by respiratory system / Mitochondrial protein import / gliogenesis / neural precursor cell proliferation / [2Fe-2S] cluster assembly / mitochondrial respirasome / NADH dehydrogenase activity / cardiac muscle tissue development / Glyoxylate metabolism and glycine degradation / oxygen sensor activity / cellular respiration / ubiquinone binding / cellular response to glucocorticoid stimulus / acyl binding / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / mitochondrial ribosome / electron transport coupled proton transport / iron-sulfur cluster assembly / mitochondrial ATP synthesis coupled electron transport / acyl carrier activity / azurophil granule membrane / mitochondrial translation / NADH:ubiquinone reductase (H+-translocating) / sodium ion transport / 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 / NADH dehydrogenase (ubiquinone) activity / RHOG GTPase cycle / quinone binding / ATP synthesis coupled electron transport / cellular response to interferon-beta / negative regulation of intrinsic apoptotic signaling pathway / 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 / respiratory electron transport chain / cerebellum development / neurogenesis / response to cocaine / regulation of mitochondrial membrane potential / response to nicotine / synaptic membrane / fatty acid binding / apoptotic signaling pathway / mitochondrial membrane / sensory perception of sound / regulation of protein phosphorylation / brain development / response to hydrogen peroxide / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / negative regulation of cell growth / circadian rhythm / fatty acid biosynthetic process / positive regulation of protein catabolic process / NAD binding / positive regulation of fibroblast proliferation / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / response to ethanol / response to oxidative stress / mitochondrial inner membrane / in utero embryonic development / protease binding / electron transfer activity / response to hypoxia / nuclear body / mitochondrial matrix / structural constituent of ribosome / nuclear speck / negative regulation of DNA-templated transcription / neuronal cell body / ubiquitin protein ligase binding / calcium ion binding / Neutrophil degranulation / protein-containing complex binding Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 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_6773.map.gz | 26.2 MB | EMDB map data format | |
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Header (meta data) | emd-6773-v30.xml emd-6773.xml | 14.3 KB 14.3 KB | Display Display | EMDB header |
Images | emd_6773.png | 23.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6773 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6773 | HTTPS FTP |
-Related structure data
Related structure data | 5xtdMC 6771C 6772C 6774C 6775C 6776C 5xtbC 5xtcC 5xteC 5xthC 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_6773.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | This map was obtained by sub-region refinement. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 complex I
Entire | Name: Human respiratory complex I |
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Components |
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-Supramolecule #1: Human respiratory complex I
Supramolecule | Name: Human respiratory complex I / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#44 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Experimental: 1.0 MDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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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: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 167761 |