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Yorodumi- PDB-9i1w: High resolution structure of the thermophilic 60S ribosomal subun... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9i1w | ||||||||||||||||||||||||
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| Title | High resolution structure of the thermophilic 60S ribosomal subunit of Chaetomium thermophilum | ||||||||||||||||||||||||
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Keywords | RIBOSOME / 60S ribosomal subunit thermophilic eukaryote RNA modification pseudouridine | ||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of cytoplasmic translational initiation / RNA polymerase I core factor complex / dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / oligosaccharyltransferase complex / preribosome / : / RNA polymerase I core promoter sequence-specific DNA binding / nucleolar large rRNA transcription by RNA polymerase I / ribosomal large subunit export from nucleus ...regulation of cytoplasmic translational initiation / RNA polymerase I core factor complex / dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / oligosaccharyltransferase complex / preribosome / : / RNA polymerase I core promoter sequence-specific DNA binding / nucleolar large rRNA transcription by RNA polymerase I / ribosomal large subunit export from nucleus / protein kinase activator activity / protein-RNA complex assembly / post-translational protein modification / cellular response to amino acid starvation / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / large ribosomal subunit / ribosome biogenesis / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / protein ubiquitination / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / metal ion binding / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Thermochaetoides thermophila DSM 1495 (fungus) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.38 Å | ||||||||||||||||||||||||
Authors | Wild, K. / Klein, M.A. / Sinning, I. | ||||||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: Nucleic Acids Res / Year: 2025Title: Pseudouridine increases ribosome stability in a thermophilic eukaryote. Authors: Klemens Wild / Marius Klein / Alicia Burkard / Virginie Marchand / Nikola Kellner / Antonio Paez / Stefan Pastore / Tamer Butto / Yuri Motorin / Mark Helm / Irmgard Sinning / ![]() Abstract: RNA modifications alter stability, folding space, and interaction network of RNA molecules. Ribosomal RNA (rRNA) modifications stabilize the structure of ribosomes and cluster around functionally ...RNA modifications alter stability, folding space, and interaction network of RNA molecules. Ribosomal RNA (rRNA) modifications stabilize the structure of ribosomes and cluster around functionally important sites such as the peptidyl transferase center, ribosomal subunit bridges, and the polypeptide tunnel. Here, we investigate the rRNA modifications of the thermophilic fungus Chaetomium thermophilum (ct), a model organism for eukaryotic thermophily and structural stability. Using LC-MS/MS, orthogonal second and third generation RNA-sequencing and high-resolution cryo-electron microscopy, we describe a cross-correlating method to assign and quantify all ct rRNA modifications. Overall, a doubling of rRNA modifications to 4% explains ribosomal thermostability with an extended distribution towards peripheral functional sites. The 2.4 Å structure of the idle ct60S ribosome, retaining nascent chains and including metal ions, polyamines, and water molecules, allows for a comprehensive structure-function analysis. Comparison with mesophilic ribosomes from Chaetomium globosum, yeast, and human highlights the significant increase of pseudouridines (Ψs). The number of Ψs linearly correlates with growth temperature, suggesting statistical modification. A ct-specific Ψ substitution forming a 'Ψ-turn' at the polypeptide tunnel exit close to the third constriction exemplifies mechanistic adaptations of the ribosome at elevated temperatures. | ||||||||||||||||||||||||
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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 | 9i1w.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9i1w.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9i1w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i1/9i1w ftp://data.pdbj.org/pub/pdb/validation_reports/i1/9i1w | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52576MC 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
-RNA chain , 4 types, 4 molecules 1349
| #1: RNA chain | Mass: 1079529.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
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| #2: RNA chain | Mass: 38612.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
| #3: RNA chain | Mass: 50161.715 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
| #4: RNA chain | Mass: 894.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
+60S ribosomal protein ... , 32 types, 33 molecules LALBLCLDLELFLGLHLILKLLLMLOLPLSLTLULVLWLXLYLZLaLbLcLeLfLiLkLn...
-Putative ribosomal ... , 2 types, 2 molecules LJLm
| #14: Protein | Mass: 20119.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0SHQ2 |
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| #43: Protein | Mass: 14609.222 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0S8G4 |
-Ribosomal protein ... , 6 types, 6 molecules LNLQLRLgLjLl
| #18: Protein | Mass: 24307.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0RZ88 |
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| #21: Protein | Mass: 24195.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0S9B5 |
| #22: Protein | Mass: 22409.201 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0S9T3 |
| #37: Protein | Mass: 13492.993 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0SFN0 |
| #40: Protein | Mass: 10660.455 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0S101 |
| #42: Protein | Mass: 12577.054 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
-Putative 60S ribosomal ... , 2 types, 2 molecules LdLq
| #34: Protein | Mass: 13872.177 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0SD68 |
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| #47: Protein | Mass: 15960.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0SHJ6 |
-Protein , 2 types, 2 molecules LhLs
| #38: Protein | Mass: 14643.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0S0D7, dolichyl-diphosphooligosaccharide-protein glycotransferase |
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| #48: Protein | Mass: 33853.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus)References: UniProt: G0SGP3 |
-Nascent chain ... , 2 types, 2 molecules PCPN
| #49: Protein/peptide | Mass: 188.225 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
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| #50: Protein/peptide | Mass: 528.644 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermochaetoides thermophila DSM 1495 (fungus) |
-Non-polymers , 6 types, 2692 molecules 










| #51: Chemical | | #52: Chemical | #53: Chemical | ChemComp-MG / #54: Chemical | ChemComp-K / #55: Chemical | ChemComp-ZN / #56: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-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: 60S subunit / Type: RIBOSOME / Entity ID: #1-#50 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2100 nm / Nominal defocus min: 1100 nm |
| Image recording | Electron dose: 42.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21_5207: / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 2.38 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 653542 / Symmetry type: POINT |
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Thermochaetoides thermophila DSM 1495 (fungus)
Germany, 1items
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