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Yorodumi- EMDB-23416: Locally filtered map of yeast III-IV supercomplex with cytochrome c -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-23416 | |||||||||
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Title | Locally filtered map of yeast III-IV supercomplex with cytochrome c | |||||||||
Map data | Locally filtered map of yeast III-IV supercomplex with cytochrome c | |||||||||
Sample |
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Function / homology | Function and homology information : / Complex III assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / mitochondrial cytochrome c oxidase assembly / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respirasome assembly / Mitochondrial protein degradation / : ...: / Complex III assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / mitochondrial cytochrome c oxidase assembly / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respirasome assembly / Mitochondrial protein degradation / : / : / : / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / cellular respiration / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial crista / electron transport coupled proton transport / ATP synthesis coupled electron transport / enzyme regulator activity / aerobic respiration / nuclear periphery / proton transmembrane transport / mitochondrial membrane / metalloendopeptidase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / proteolysis / zinc ion binding / membrane / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||
Authors | Moe A / Di Trani J / Rubinstein J / Brzezinski P | |||||||||
Funding support | Canada, Sweden, 2 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2021 Title: Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochrome in the yeast III-IV respiratory supercomplex. Authors: Agnes Moe / Justin Di Trani / John L Rubinstein / Peter Brzezinski / Abstract: Energy conversion in aerobic organisms involves an electron current from low-potential donors, such as NADH and succinate, to dioxygen through the membrane-bound respiratory chain. Electron transfer ...Energy conversion in aerobic organisms involves an electron current from low-potential donors, such as NADH and succinate, to dioxygen through the membrane-bound respiratory chain. Electron transfer is coupled to transmembrane proton transport, which maintains the electrochemical proton gradient used to produce ATP and drive other cellular processes. Electrons are transferred from respiratory complexes III to IV (CIII and CIV) by water-soluble cytochrome (cyt.) In and some other organisms, these complexes assemble into larger CIIICIV supercomplexes, the functional significance of which has remained enigmatic. In this work, we measured the kinetics of the supercomplex cyt. -mediated QH:O oxidoreductase activity under various conditions. The data indicate that the electronic link between CIII and CIV is confined to the surface of the supercomplex. Single-particle electron cryomicroscopy (cryo-EM) structures of the supercomplex with cyt. show the positively charged cyt. bound to either CIII or CIV or along a continuum of intermediate positions. Collectively, the structural and kinetic data indicate that cyt. travels along a negatively charged patch on the supercomplex surface. Thus, rather than enhancing electron transfer rates by decreasing the distance that cyt. must diffuse in three dimensions, formation of the CIIICIV supercomplex facilitates electron transfer by two-dimensional (2D) diffusion of cyt. This mechanism enables the CIIICIV supercomplex to increase QH:O oxidoreductase activity and suggests a possible regulatory role for supercomplex formation in the respiratory chain. | |||||||||
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_23416.map.gz | 12 MB | EMDB map data format | |
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Header (meta data) | emd-23416-v30.xml emd-23416.xml | 8.1 KB 8.1 KB | Display Display | EMDB header |
Images | emd_23416.png | 41.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-23416 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-23416 | HTTPS FTP |
-Validation report
Summary document | emd_23416_validation.pdf.gz | 302.3 KB | Display | EMDB validaton report |
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Full document | emd_23416_full_validation.pdf.gz | 301.9 KB | Display | |
Data in XML | emd_23416_validation.xml.gz | 7.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-23416 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-23416 | HTTPS FTP |
-Related structure data
Related structure data | 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_23416.map.gz / Format: CCP4 / Size: 209.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Locally filtered map of yeast III-IV supercomplex with cytochrome c | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.03 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 : yeast III-IV supercomplex with cytochrome c
Entire | Name: yeast III-IV supercomplex with cytochrome c |
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Components |
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-Supramolecule #1: yeast III-IV supercomplex with cytochrome c
Supramolecule | Name: yeast III-IV supercomplex with cytochrome c / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
-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-PROPANE |
Details | monodisperse |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 42.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2) / Number images used: 73542 |
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Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |