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Yorodumi- PDB-6rfq: Cryo-EM structure of a respiratory complex I assembly intermediat... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6rfq | |||||||||||||||||||||
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| Title | Cryo-EM structure of a respiratory complex I assembly intermediate with NDUFAF2 | |||||||||||||||||||||
Components |
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Keywords | OXIDOREDUCTASE / Complex I / NADH dehydrogenase / Mitochondrion Proton pumping / Ubiquinone | |||||||||||||||||||||
| Function / homology | Function and homology informationlipoate biosynthetic process / NADH dehydrogenase / TIM23 mitochondrial import inner membrane translocase complex / membrane protein complex / NADH dehydrogenase complex / ubiquinone biosynthetic process / mitochondrial [2Fe-2S] assembly complex / oxidoreductase activity, acting on NAD(P)H / NADH dehydrogenase activity / iron-sulfur cluster assembly ...lipoate biosynthetic process / NADH dehydrogenase / TIM23 mitochondrial import inner membrane translocase complex / membrane protein complex / NADH dehydrogenase complex / ubiquinone biosynthetic process / mitochondrial [2Fe-2S] assembly complex / oxidoreductase activity, acting on NAD(P)H / NADH dehydrogenase activity / iron-sulfur cluster assembly / ubiquinone binding / electron transport coupled proton transport / acyl binding / protein import into mitochondrial matrix / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / catalytic complex / quinone binding / ATP synthesis coupled electron transport / aerobic respiration / respiratory electron transport chain / electron transport chain / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / mitochondrial membrane / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / oxidoreductase activity / mitochondrial inner membrane / protein-containing complex binding / mitochondrion / metal ion binding / membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | Yarrowia lipolytica (yeast) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||
Authors | Parey, K. / Vonck, J. | |||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: Sci Adv / Year: 2019Title: High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease. Authors: Kristian Parey / Outi Haapanen / Vivek Sharma / Harald Köfeler / Thomas Züllig / Simone Prinz / Karin Siegmund / Ilka Wittig / Deryck J Mills / Janet Vonck / Werner Kühlbrandt / Volker Zickermann / ![]() Abstract: Respiratory complex I is a redox-driven proton pump, accounting for a large part of the electrochemical gradient that powers mitochondrial adenosine triphosphate synthesis. Complex I dysfunction is ...Respiratory complex I is a redox-driven proton pump, accounting for a large part of the electrochemical gradient that powers mitochondrial adenosine triphosphate synthesis. Complex I dysfunction is associated with severe human diseases. Assembly of the one-megadalton complex I in the inner mitochondrial membrane requires assembly factors and chaperones. We have determined the structure of complex I from the aerobic yeast by electron cryo-microscopy at 3.2-Å resolution. A ubiquinone molecule was identified in the access path to the active site. The electron cryo-microscopy structure indicated an unusual lipid-protein arrangement at the junction of membrane and matrix arms that was confirmed by molecular simulations. The structure of a complex I mutant and an assembly intermediate provide detailed molecular insights into the cause of a hereditary complex I-linked disease and complex I assembly in the inner mitochondrial membrane. | |||||||||||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6rfq.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6rfq.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 6rfq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6rfq_validation.pdf.gz | 2.8 MB | Display | wwPDB validaton report |
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| Full document | 6rfq_full_validation.pdf.gz | 3 MB | Display | |
| Data in XML | 6rfq_validation.xml.gz | 225.6 KB | Display | |
| Data in CIF | 6rfq_validation.cif.gz | 335.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rf/6rfq ftp://data.pdbj.org/pub/pdb/validation_reports/rf/6rfq | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4872MC ![]() 4873C ![]() 4874C ![]() 6rfrC ![]() 6rfsC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Protein , 39 types, 39 molecules ABCDEFGHIJKLPRSUWXYZabcdefgijk...
-Acyl carrier protein ... , 2 types, 2 molecules OQ
| #13: Protein | Mass: 12053.585 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Yarrowia lipolytica (yeast) / References: UniProt: A0A1H6PXT9, UniProt: Q6C926*PLUS |
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| #15: Protein | Mass: 14444.458 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Yarrowia lipolytica (yeast) / References: UniProt: A0A1D8NG21, UniProt: Q6C7X2*PLUS |
-Non-polymers , 11 types, 36 molecules 




















| #42: Chemical | ChemComp-SF4 / #43: Chemical | #44: Chemical | ChemComp-FMN / | #45: Chemical | ChemComp-NDP / | #46: Chemical | ChemComp-3PE / #47: Chemical | #48: Chemical | ChemComp-CDL / #49: Chemical | #50: Chemical | ChemComp-PLC / #51: Chemical | #52: Chemical | ChemComp-CPL / | |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Complex I assembly intermediate / Type: COMPLEX / Entity ID: #1-#41 / Source: NATURAL |
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| Source (natural) | Organism: Yarrowia lipolytica (yeast) / Strain: GB20 |
| Buffer solution | pH: 7.2 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: C-flat-1.2/1.3 4C |
| Vitrification | Cryogen name: ETHANE |
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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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 130000 X / Calibrated magnification: 46425 X / Calibrated defocus min: 1500 nm / Calibrated defocus max: 2500 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 8 sec. / Electron dose: 40 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 1386 |
| EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
| Image scans | Movie frames/image: 40 |
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Processing
| Software | Name: PHENIX / Version: 1.12_2829: / Classification: refinement | ||||||||||||||||||||||||||||||||
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| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 250406 | ||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 112418 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: OTHER / Space: REAL | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 3.3 Å | ||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Yarrowia lipolytica (yeast)
Germany, 1items
Citation

UCSF Chimera

















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