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Yorodumi- PDB-8p5d: Spraguea lophii ribosome in the closed conformation by cryo sub t... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8p5d | |||||||||
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| Title | Spraguea lophii ribosome in the closed conformation by cryo sub tomogram averaging | |||||||||
Components |
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Keywords | RIBOSOME / Microsporidia | |||||||||
| Function / homology | Function and homology informationpreribosome / nonfunctional rRNA decay / preribosome, small subunit precursor / translational elongation / translational termination / ribosomal subunit export from nucleus / ribosomal small subunit export from nucleus / translation regulator activity / DNA-(apurinic or apyrimidinic site) endonuclease activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ...preribosome / nonfunctional rRNA decay / preribosome, small subunit precursor / translational elongation / translational termination / ribosomal subunit export from nucleus / ribosomal small subunit export from nucleus / translation regulator activity / DNA-(apurinic or apyrimidinic site) endonuclease activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / maintenance of translational fidelity / rRNA processing / large ribosomal subunit / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleus / membrane / cytosol Similarity search - Function | |||||||||
| Biological species | Spraguea lophii 42_110 (fungus) | |||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 10.8 Å | |||||||||
Authors | Gil Diez, P. / McLaren, M. / Isupov, M.N. / Daum, B. / Conners, R. / Williams, B. | |||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Nat Microbiol / Year: 2023Title: CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state. Authors: Mathew McLaren / Rebecca Conners / Michail N Isupov / Patricia Gil-Díez / Lavinia Gambelli / Vicki A M Gold / Andreas Walter / Sean R Connell / Bryony Williams / Bertram Daum / ![]() Abstract: Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be ...Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography and single-particle electron cryo-microscopy. We show that microsporidian spores contain hibernating ribosomes that are locked in a dimeric (100S) state, which is formed by a unique dimerization mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerization acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilize this mechanism in translational control. | |||||||||
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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 | 8p5d.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8p5d.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8p5d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8p5d_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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| Full document | 8p5d_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 8p5d_validation.xml.gz | 323.9 KB | Display | |
| Data in CIF | 8p5d_validation.cif.gz | 534.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p5/8p5d ftp://data.pdbj.org/pub/pdb/validation_reports/p5/8p5d | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 17448MC ![]() 8p60C ![]() 16198 C: citing same article ( M: map data used to model this data |
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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
-RNA chain , 3 types, 3 molecules L50L70S60
| #1: RNA chain | Mass: 849039.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
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| #2: RNA chain | Mass: 38356.801 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #42: RNA chain | Mass: 444812.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
+60S ribosomal protein ... , 27 types, 27 molecules LA0LB0LC0LCCLD0LDDLE0LEELF0LFFLG0LH0LIILJ0LL0LLLLOOLP0LPPLQ0LR0LS0LT0LU0LX0LY0LZ0
-Protein , 15 types, 15 molecules LAALHHLI0LJJLM0LMMMD1SB0SBBSCCSEESFFSGGSR0SX0
| #4: Protein | Mass: 16609.498 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
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| #17: Protein | Mass: 14183.866 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7W7Y2 |
| #18: Protein | Mass: 25142.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7WBF8 |
| #21: Protein | Mass: 10517.657 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #24: Protein | Mass: 13258.343 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XVN9 |
| #25: Protein | Mass: 14563.868 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XSQ3 |
| #41: Protein | Mass: 17595.088 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7W5K5 |
| #45: Protein | Mass: 25934.658 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #46: Protein | Mass: 9189.923 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #48: Protein | Mass: 7288.479 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #52: Protein | Mass: 6816.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #54: Protein | Mass: 16937.791 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7W9X5 |
| #56: Protein | Mass: 36182.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XVG3 |
| #67: Protein | Mass: 14055.251 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
| #73: Protein | Mass: 15822.722 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) |
-Ribosomal protein ... , 7 types, 7 molecules LGGLN0LO0LV0LW0SP0SV0
| #15: Protein | Mass: 12020.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7W7C6 |
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| #26: Protein | Mass: 24200.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7W7A2 |
| #27: Protein | Mass: 22885.139 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XUD8 |
| #36: Protein | Mass: 15239.987 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XLC4 |
| #37: Protein | Mass: 15342.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XSY2 |
| #65: Protein | Mass: 18514.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7XKY9 |
| #71: Protein | Mass: 7768.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Spraguea lophii 42_110 (fungus) / References: UniProt: S7WAC1 |
+40S ribosomal protein ... , 23 types, 23 molecules SA0SAASC0SD0SDDSE0SF0SG0SH0SI0SJ0SK0SL0SM0SN0SO0SQ0SS0ST0SU0SW0SY0SZ0
-Non-polymers , 1 types, 9 molecules 
| #76: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging |
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Sample preparation
| Component | Name: Ribosome / Type: RIBOSOME / Entity ID: #1-#64, #66-#75, #65 / Source: NATURAL |
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| Source (natural) | Organism: Spraguea lophii 42_110 (fungus) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Details: 20 mA, Carbon coated grid / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 288.15 K / Details: blot force -1 and blot time 4 s |
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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 defocus max: 6000 nm / Nominal defocus min: 2500 nm / Cs: 2.7 mm | ||||||||||||||||||
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER | ||||||||||||||||||
| Image recording |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 10.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1344 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| EM volume selection | Num. of tomograms: 20 / Num. of volumes extracted: 6505 | ||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 10.8 Å |
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About Yorodumi



Spraguea lophii 42_110 (fungus)
United Kingdom, 1items
Citation






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FIELD EMISSION GUN