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Yorodumi- EMDB-15900: Subtomogram average of the respiratory supercomplex from Tetrahym... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15900 | |||||||||||||||
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Title | Subtomogram average of the respiratory supercomplex from Tetrahymena thermophila mitochondria | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Biological species | Tetrahymena thermophila (eukaryote) | |||||||||||||||
Method | subtomogram averaging / cryo EM / Resolution: 28.0 Å | |||||||||||||||
Authors | Muhleip A / Amunts A | |||||||||||||||
Funding support | Sweden, European Union, 4 items
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Citation | Journal: Nature / Year: 2023 Title: Structural basis of mitochondrial membrane bending by the I-II-III-IV supercomplex. Authors: Alexander Mühleip / Rasmus Kock Flygaard / Rozbeh Baradaran / Outi Haapanen / Thomas Gruhl / Victor Tobiasson / Amandine Maréchal / Vivek Sharma / Alexey Amunts / Abstract: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes ...Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III-IV supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization. | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_15900.map.gz | 37.7 MB | EMDB map data format | |
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Header (meta data) | emd-15900-v30.xml emd-15900.xml | 20.4 KB 20.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_15900_fsc.xml | 10.2 KB | Display | FSC data file |
Images | emd_15900.png | 101.7 KB | ||
Masks | emd_15900_msk_1.map | 40.6 MB | Mask map | |
Others | emd_15900_half_map_1.map.gz emd_15900_half_map_2.map.gz | 37.6 MB 37.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15900 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15900 | HTTPS FTP |
-Validation report
Summary document | emd_15900_validation.pdf.gz | 1.4 MB | Display | EMDB validaton report |
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Full document | emd_15900_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | emd_15900_validation.xml.gz | 13.7 KB | Display | |
Data in CIF | emd_15900_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15900 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15900 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_15900.map.gz / Format: CCP4 / Size: 40.6 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: 4.22 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_15900_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_15900_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_15900_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : mitochondrial membranes from Tetrahymena thermophila
Entire | Name: mitochondrial membranes from Tetrahymena thermophila |
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Components |
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-Supramolecule #1: mitochondrial membranes from Tetrahymena thermophila
Supramolecule | Name: mitochondrial membranes from Tetrahymena thermophila / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1-#53 |
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Source (natural) | Organism: Tetrahymena thermophila (eukaryote) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
Aggregation state | 3D array |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 3.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |