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Yorodumi- PDB-9f62: Subtomogram average of the Chlamydomonas reinhardtii mitochondria... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9f62 | ||||||||||||||||||||||||||||||
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| Title | Subtomogram average of the Chlamydomonas reinhardtii mitochondrial respirasome I2 III4 IV6 | ||||||||||||||||||||||||||||||
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Keywords | MEMBRANE PROTEIN / respirasome / alga / respiration / mitochondria | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationquinol-cytochrome-c reductase / TIM22 mitochondrial import inner membrane insertion complex / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase / mitochondrial processing peptidase / mitochondrion targeting sequence binding / protein insertion into mitochondrial inner membrane / NADH dehydrogenase complex / ubiquinone biosynthetic process / respiratory chain complex IV ...quinol-cytochrome-c reductase / TIM22 mitochondrial import inner membrane insertion complex / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase / mitochondrial processing peptidase / mitochondrion targeting sequence binding / protein insertion into mitochondrial inner membrane / NADH dehydrogenase complex / ubiquinone biosynthetic process / respiratory chain complex IV / mitochondrial envelope / cytochrome-c oxidase / respiratory chain complex III / oxidative phosphorylation / quinol-cytochrome-c reductase / mitochondrial electron transport, cytochrome c to oxygen / oxidoreductase activity, acting on NAD(P)H / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / acyl binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / phosphopantetheine binding / respiratory chain complex I / protein transmembrane transporter activity / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / proton transmembrane transport / aerobic respiration / respiratory electron transport chain / electron transport chain / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / metallopeptidase activity / FMN binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / mitochondrial inner membrane / copper ion binding / heme binding / protein-containing complex binding / mitochondrion / metal ion binding / membrane Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 5.44 Å | ||||||||||||||||||||||||||||||
Authors | Waltz, F. / Righetto, R. / Kotecha, A. / Engel, B.D. | ||||||||||||||||||||||||||||||
| Funding support | Germany, Switzerland, 2items
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Citation | Journal: Science / Year: 2025Title: In-cell architecture of the mitochondrial respiratory chain. Authors: Florent Waltz / Ricardo D Righetto / Lorenz Lamm / Thalia Salinas-Giegé / Ron Kelley / Xianjun Zhang / Martin Obr / Sagar Khavnekar / Abhay Kotecha / Benjamin D Engel / ![]() Abstract: Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, ...Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, working in concert to transfer electrons and pump protons. The precise organization of these complexes in native cells is debated. We used in situ cryo-electron tomography to visualize the native structures and organization of several major mitochondrial complexes in cells. ATP synthases and respiratory complexes segregate into curved and flat crista membrane domains, respectively. Respiratory complexes I, III, and IV assemble into a respirasome supercomplex, from which we determined a native 5-angstrom (Å) resolution structure showing binding of electron carrier cytochrome . Combined with single-particle cryo-electron microscopy at 2.4-Å resolution, we model how the respiratory complexes organize inside native mitochondria. | ||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9f62.cif.gz | 6.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9f62.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9f62.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9f62_validation.pdf.gz | 4.5 MB | Display | wwPDB validaton report |
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| Full document | 9f62_full_validation.pdf.gz | 4.6 MB | Display | |
| Data in XML | 9f62_validation.xml.gz | 790.7 KB | Display | |
| Data in CIF | 9f62_validation.cif.gz | 1.3 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f6/9f62 ftp://data.pdbj.org/pub/pdb/validation_reports/f6/9f62 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 50210MC ![]() 9f5xC ![]() 9f5yC ![]() 9f5zC ![]() 9f60C ![]() 9f61C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Protein , 27 types, 98 molecules 1A1B6A6B1E1F6E6F1G1H6G6H1M1N6M6N1Q1S6Q6S2C3C4C7C8C9C2E3E4E7E...
+Cytochrome b-c1 complex subunit ... , 3 types, 12 molecules 1C1D6C6D1I1J6I6J1R1T6R6T
+Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit ... , 2 types, 8 molecules 1K1L6K6L1O1P6O6P
+Cytochrome c oxidase ... , 4 types, 24 molecules 2A3A4A7A8A9A2B3B4B7B8B9B2D3D4D7D8D9D2J3J4J7J8J9J
+NADH:ubiquinone oxidoreductase ... , 11 types, 22 molecules 5AA5CC5DD5EE5FF5GG5KK5MM5OO5ii5ll
+NADH dehydrogenase [ubiquinone] ... , 6 types, 12 molecules 5BB5LL5NN5jj5kk5mm
+Mitochondrial NADH:ubiquinone oxidoreductase ... , 9 types, 18 molecules 5II5dd5ee5ff5hh5pp5qq5ss5ww
+Putative NADH:ubiquinone oxidoreductase ... , 3 types, 6 molecules 5PP5nn5oo
+NADH-ubiquinone oxidoreductase chain ... , 6 types, 12 molecules 5QQ5RR5SS5TT5VV5WW
+Protein/peptide , 1 types, 2 molecules 5vv
+Non-polymers , 13 types, 74 molecules 
























+Details
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
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Sample preparation
| Component | Name: Chlamydomonas reinhardtii / Type: CELL / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 64000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 800 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 3.5 e/Å2 / Avg electron dose per subtomogram: 143.5 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
| EM imaging optics | Energyfilter name: TFS Selectris X |
| Image scans | Width: 4096 / Height: 4096 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 5.44 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 14488 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| EM volume selection | Method: Template Matching / Num. of tomograms: 131 / Num. of volumes extracted: 26591 |
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Germany,
Switzerland, 2items
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