+Open data
-Basic information
Entry | Database: PDB / ID: 6qc3 | ||||||
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Title | Ovine respiratory supercomplex I+III2 open class 1 | ||||||
Components |
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Keywords | ELECTRON TRANSPORT / supercomplex / cellular respiration / mitochondria | ||||||
Function / homology | Function and homology information : / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / NADH dehydrogenase activity / : / mitochondrial respiratory chain complex I assembly ...: / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / NADH dehydrogenase activity / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / membrane => GO:0016020 / : / ATP metabolic process / respiratory electron transport chain / reactive oxygen species metabolic process / FAD binding / regulation of mitochondrial membrane potential / electron transport chain / metalloendopeptidase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / circadian rhythm / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / electron transfer activity / oxidoreductase activity / mitochondrial matrix / heme binding / protein-containing complex binding / proteolysis / nucleoplasm / metal ion binding Similarity search - Function | ||||||
Biological species | Ovis aries (sheep) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å | ||||||
Authors | Letts, J.A. / Sazanov, L.A. | ||||||
Funding support | Austria, 1items
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Citation | Journal: Mol Cell / Year: 2019 Title: Structures of Respiratory Supercomplex I+III Reveal Functional and Conformational Crosstalk. Authors: James A Letts / Karol Fiedorczuk / Gianluca Degliesposti / Mark Skehel / Leonid A Sazanov / Abstract: The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We ...The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII. CI shows a transition between "closed" and "open" conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII, suggesting that interaction with CI disrupts CIII symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6qc3.cif.gz | 2.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6qc3.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6qc3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6qc3_validation.pdf.gz | 3 MB | Display | wwPDB validaton report |
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Full document | 6qc3_full_validation.pdf.gz | 3.1 MB | Display | |
Data in XML | 6qc3_validation.xml.gz | 316.5 KB | Display | |
Data in CIF | 6qc3_validation.cif.gz | 487.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qc/6qc3 ftp://data.pdbj.org/pub/pdb/validation_reports/qc/6qc3 | HTTPS FTP |
-Related structure data
Related structure data | 4495MC 4479C 4480C 4481C 4482C 4493C 4494C 4496C 4497C 4498C 4499C 4500C 4501C 4502C 4505C 4506C 4507C 6q9bC 6q9dC 6q9eC 6qa9C 6qbxC 6qc2C 6qc4C 6qc5C 6qc6C 6qc7C 6qc8C 6qc9C 6qcaC 6qcfC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
+Protein , 17 types, 24 molecules a1a3b1b2c1c2d1d2h1h2i1i2S2S7S8V3S6AAABBJC2AMB1A1
+Ubiquinol-cytochrome c reductase ... , 2 types, 4 molecules a2a4q1q2
+Cytochrome b-c1 complex subunit Rieske, ... , 2 types, 4 molecules f1f2x1x2
+NADH dehydrogenase [ubiquinone] flavoprotein ... , 2 types, 2 molecules V1V2
+NADH:ubiquinone oxidoreductase core subunit ... , 2 types, 2 molecules S1S3
+NADH:ubiquinone oxidoreductase subunit ... , 11 types, 11 molecules S4A9A6B5S5A3B3B4B7B9B2
+NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 7 types, 7 molecules A2A5A7ALAKA8AJ
+NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules D3D1D64LD5D4D2
+NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 3 types, 3 molecules B6B8BK
+Protein/peptide , 1 types, 1 molecules C1
+Non-polymers , 11 types, 28 molecules
+Details
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Ovine mitochondrial respiratory supercomplex I+III2 / Type: COMPLEX / Details: Open class 1 from ovine respiratory SC I+III2 / Entity ID: #1-#54 / Source: NATURAL | ||||||||||||||||||||
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Molecular weight | Value: 1.4 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: Ovis aries (sheep) / Cellular location: Mitochondrial inner membrane / Organ: Heart / Organelle: Mitochondria / Tissue: Cardiac | ||||||||||||||||||||
Buffer solution | pH: 7.4 / Details: 250 mM NaCl, 20 mM HEPES, pH 7.7, 0.02% Brij-35 | ||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: PROPANE / Humidity: 95 % / Chamber temperature: 277 K Details: blotting for 30 seconds at 4 degrees Celsius, 95% humidity and flash freezing |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
Electron lens | Mode: BRIGHT FIELD / Calibrated magnification: 100000 X / Calibrated defocus min: 1500 nm / Calibrated defocus max: 3000 nm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 2 sec. / Electron dose: 51 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 1854 |
Image scans | Movie frames/image: 34 |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 400000 | ||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35640 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | B value: 90 / Protocol: OTHER / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 1PPJ Accession code: 1PPJ / Source name: PDB / Type: experimental model |