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Yorodumi- PDB-9phc: In vitro reconstituted complex of purified S. pombe large ribosom... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9phc | |||||||||||||||||||||||||||
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| Title | In vitro reconstituted complex of purified S. pombe large ribosomal subunit and SNOR | |||||||||||||||||||||||||||
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Keywords | RIBOSOME / 60S / large subunit / SNOR / pombe / Yeast / Hibernating / Glucose | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationL13a-mediated translational silencing of Ceruloplasmin expression / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / SRP-dependent cotranslational protein targeting to membrane / ribonuclease MRP complex / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / preribosome / tRNA processing / cytosolic large ribosomal subunit assembly ...L13a-mediated translational silencing of Ceruloplasmin expression / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / SRP-dependent cotranslational protein targeting to membrane / ribonuclease MRP complex / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / preribosome / tRNA processing / cytosolic large ribosomal subunit assembly / pre-mRNA intronic binding / protein-RNA complex assembly / maturation of LSU-rRNA / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / rRNA processing / ribosome biogenesis / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / negative regulation of gene expression / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleus / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||||||||||||||||||||
Authors | Gluc, M. / Jomaa, A. | |||||||||||||||||||||||||||
| Funding support | United States, Germany, 2items
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Citation | Journal: Nature / Year: 2026Title: SNOR promotes translation restart after dormancy. Authors: Maciej Gluc / Higor Rosa / Maria Bozko / Lesley A Turner / Cassidy R Prince / Yelena Peskova / Heather A Feaga / Kathleen L Gould / Simone Mattei / Ahmad Jomaa / ![]() Abstract: Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis. How inactive eukaryotic ribosomes are reactivated when nutrients return remains ...Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis. How inactive eukaryotic ribosomes are reactivated when nutrients return remains unclear. Here, using high-resolution in situ cryo-electron tomography in Schizosaccharomyces pombe, we identify SNOR, an SBDS domain-containing ribosome-associated factor that binds at the peptidyl transferase centre and contacts the hypusinated loop of eIF5A during glucose depletion-induced dormancy. Rather than acting as a canonical hibernation factor, SNOR licenses dormant ribosomes for rapid translational restart. Upon glucose repletion, SNOR and eIF5A act together to promote efficient recovery of polysomes and exit from dormancy. These findings define a stress-responsive ribosome restart module that couples carbon-source limitation to surveillance of the ribosomal active site and reactivation of protein synthesis. | |||||||||||||||||||||||||||
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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 | 9phc.cif.gz | 3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9phc.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9phc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ph/9phc ftp://data.pdbj.org/pub/pdb/validation_reports/ph/9phc | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 71645MC ![]() 9rvuC 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
+Large ribosomal subunit protein ... , 40 types, 40 molecules B0B1BNBOBPBQBRBSBTBUBVBWBXBYBZBaBbBcBdBeBfBgBhBiBjBkBlBmBnBo...
-RNA chain , 3 types, 3 molecules B2B3B4
| #3: RNA chain | Mass: 1129828.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: RNA chain | Mass: 78518.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: RNA chain | Mass: 52880.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein / Non-polymers , 2 types, 4 molecules HS

| #44: Protein | Mass: 11909.361 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SPBC21C3.19 Production host: ![]() References: UniProt: Q9P7K6 |
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| #45: Chemical |
-Details
| Has ligand of interest | N |
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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: single particle reconstruction |
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Sample preparation
| Component | Name: In vitro reconstituted complex of purified S. pombe large ribosomal subunit and SNOR Type: RIBOSOME / Entity ID: #1-#44 / Source: MULTIPLE SOURCES |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Conc.: 0.25 mg/ml / 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 / Humidity: 100 % / Chamber temperature: 277 K |
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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: DARK FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| 3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 110548 / Symmetry type: POINT | ||||||||||||||||
| Atomic model building | Protocol: AB INITIO MODEL / Space: REAL |
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About Yorodumi





United States,
Germany, 2items
Citation




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FIELD EMISSION GUN