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Yorodumi- PDB-9t5c: Naked mole-rat 80S ribosome in post-translocation non-rotated state -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9t5c | ||||||
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| Title | Naked mole-rat 80S ribosome in post-translocation non-rotated state | ||||||
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Keywords | RIBOSOME / naked mole-rat / 80S | ||||||
| Function / homology | Function and homology informationRibosome Quality Control (RQC) complex extracts and degrades nascent peptide / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / L13a-mediated translational silencing of Ceruloplasmin expression / Translation initiation complex formation / Formation of a pool of free 40S subunits / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) ...Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / L13a-mediated translational silencing of Ceruloplasmin expression / Translation initiation complex formation / Formation of a pool of free 40S subunits / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / SRP-dependent cotranslational protein targeting to membrane / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / 5.8S rRNA binding / Translation initiation complex formation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Formation of the ternary complex, and subsequently, the 43S complex / negative regulation of protein neddylation / Formation of a pool of free 40S subunits / SRP-dependent cotranslational protein targeting to membrane / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Translation initiation complex formation / Ribosomal scanning and start codon recognition / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / Protein methylation / L13a-mediated translational silencing of Ceruloplasmin expression / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / translation at postsynapse / RMTs methylate histone arginines / A band / aminoacyl-tRNA synthetase multienzyme complex / translation at presynapse / eukaryotic 80S initiation complex / negative regulation of formation of translation preinitiation complex / axial mesoderm development / protein-DNA complex disassembly / positive regulation of respiratory burst involved in inflammatory response / 90S preribosome assembly / nucleolus organization / GAIT complex / TORC2 complex binding / middle ear morphogenesis / cytoplasmic side of rough endoplasmic reticulum membrane / cell-substrate adhesion / laminin receptor activity / homeostatic process / macrophage chemotaxis / lung morphogenesis / positive regulation of natural killer cell proliferation / basement membrane / fibroblast growth factor binding / monocyte chemotaxis / TOR signaling / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / negative regulation of respiratory burst involved in inflammatory response / ubiquitin ligase inhibitor activity / 90S preribosome / ribonucleoprotein complex binding / Viral mRNA Translation / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein localization to nucleus / negative regulation of ubiquitin-dependent protein catabolic process / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / positive regulation of signal transduction by p53 class mediator / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / protein targeting / regulation of translational fidelity / maturation of LSU-rRNA / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / protein-RNA complex assembly / Notch signaling pathway / 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) / translation regulator activity / rough endoplasmic reticulum / positive regulation of cell cycle / laminin binding / ribosomal small subunit export from nucleus / gastrulation / translation initiation factor binding / MDM2/MDM4 family protein binding / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / cellular response to interleukin-4 Similarity search - Function | ||||||
| Biological species | Heterocephalus glaber (naked mole-rat) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.89 Å | ||||||
Authors | Gul, M. / Kudryashev, M. | ||||||
| Funding support | Germany, 1items
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Citation | Journal: To Be PublishedTitle: Naked mole-rat 80S ribosome in post-translocation non-rotated state Authors: Gul, M. / Kudryashev, M. | ||||||
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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 | 9t5c.cif.gz | 5.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9t5c.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9t5c.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t5/9t5c ftp://data.pdbj.org/pub/pdb/validation_reports/t5/9t5c | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 55100MC 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 , 7 types, 7 molecules BL5L7L8S2S6S7
| #1: RNA chain | Mass: 3108.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
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| #2: RNA chain | Mass: 1531040.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
| #3: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
| #4: RNA chain | Mass: 50795.020 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
| #46: RNA chain | Mass: 603062.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
| #47: RNA chain | Mass: 24128.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
| #48: RNA chain | Mass: 24082.342 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) |
+Large ribosomal subunit protein ... , 32 types, 32 molecules LALCLDLELFLGLHLJLLLMLOLPLQLSLTLULVLWLXLYLaLbLcLdLfLgLhLkLlLpLrLB
-60S ribosomal protein ... , 6 types, 6 molecules LILZLeLiLnLo
| #12: Protein | Mass: 24657.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6QHL6 |
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| #28: Protein | Mass: 15835.831 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5BN91 |
| #33: Protein | Mass: 15898.932 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5BYD8 |
| #37: Protein | Mass: 12290.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5C0Q6 |
| #42: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6J950 |
| #43: Protein | Mass: 12476.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5BW65 |
-Ribosomal protein ... , 3 types, 3 molecules LNLRLj
| #16: Protein | Mass: 24207.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5BFP9 |
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| #20: Protein | Mass: 23535.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5BRW3 |
| #38: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6JT91 |
-Protein , 2 types, 2 molecules LmSe
| #41: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5C5A6 |
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| #78: Protein | Mass: 14441.718 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: P62862 |
+Small ribosomal subunit protein ... , 24 types, 24 molecules SASBSCSDSESFSISJSKSLSNSOSQSRSSSTSUSVSWSXSZScSdSg
-40S ribosomal protein ... , 6 types, 6 molecules SGSHSPSYSaSb
| #55: Protein | Mass: 28751.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6J125 |
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| #56: Protein | Mass: 22168.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5C7L2 |
| #63: Protein | Mass: 17076.207 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5AZL1 |
| #72: Protein | Mass: 15449.345 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PA11 |
| #74: Protein | Mass: 13063.532 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: E3VX72 |
| #75: Protein | Mass: 9480.186 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: E3VX74 |
-Non-polymers , 3 types, 337 molecules 




| #81: Chemical | ChemComp-MG / #82: Chemical | #83: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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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: 80S ribosome / Type: RIBOSOME / Entity ID: #1-#80 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Heterocephalus glaber (naked mole-rat) |
| Buffer solution | pH: 7.4 |
| 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: 3000 nm / Nominal defocus min: 1000 nm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 60.04 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| 3D reconstruction | Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 118185 / Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||
| Atomic model building | PDB-ID: 7CPU Accession code: 7CPU / Source name: PDB / Type: experimental model |
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Heterocephalus glaber (naked mole-rat)
Germany, 1items
Citation
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FIELD EMISSION GUN
