[English] 日本語
Yorodumi- PDB-9t5c: Naked mole-rat 80S ribosome in post-translocation non-rotated state -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9t5c | ||||||
|---|---|---|---|---|---|---|---|
| Title | Naked mole-rat 80S ribosome in post-translocation non-rotated state | ||||||
Components |
| ||||||
Keywords | RIBOSOME / naked mole-rat / 80S | ||||||
| Function / homology | Function and homology informationoxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein-DNA complex disassembly / protein-synthesizing GTPase / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of DNA-templated transcription initiation / negative regulation of DNA repair / supercoiled DNA binding / oxidized purine DNA binding ...oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein-DNA complex disassembly / protein-synthesizing GTPase / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of DNA-templated transcription initiation / negative regulation of DNA repair / supercoiled DNA binding / oxidized purine DNA binding / NF-kappaB complex / ubiquitin-like protein conjugating enzyme binding / laminin receptor activity / protein kinase A binding / TOR signaling / gastrulation / protein localization to nucleus / protein targeting / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of ubiquitin-dependent protein catabolic process / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / positive regulation of microtubule polymerization / spindle assembly / protein-RNA complex assembly / translation regulator activity / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / negative regulation of protein ubiquitination / positive regulation of cell cycle / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / MDM2/MDM4 family protein binding / Hsp70 protein binding / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / mRNA 3'-UTR binding / small-subunit processome / bone development / Hsp90 protein binding / positive regulation of non-canonical NF-kappaB signal transduction / base-excision repair / response to virus / mitotic spindle / cellular response to hydrogen peroxide / mRNA 5'-UTR binding / transcription coactivator binding / ruffle membrane / cytoplasmic ribonucleoprotein granule / innate immune response in mucosa / kinase activity / rRNA processing / cytosolic ribosome / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / ribosome biogenesis / 5S rRNA binding / cell body / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit rRNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / antibacterial humoral response / DNA-binding transcription factor binding / microtubule binding / cytosolic large ribosomal subunit / cell differentiation / cytoplasmic translation / protein stabilization / defense response to Gram-positive bacterium / postsynaptic density / negative regulation of translation / mitochondrial inner membrane / rRNA binding / positive regulation of apoptotic process / ribosome / translation / structural constituent of ribosome / mitochondrial matrix / ribonucleoprotein complex / ubiquitin protein ligase binding / apoptotic process / mRNA binding / centrosome / positive regulation of gene expression / positive regulation of cell population proliferation / negative regulation of apoptotic process / nucleolus / dendrite / synapse / protein kinase binding 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
| ||||||
Citation | Journal: Nat Commun / Year: 2026Title: Cryo-EM structure of the naked mole-rat ribosome reveals a stabilized split 28S rRNA. Authors: Mehmet Gül / Alice Rossi / Christian M T Spahn / Gary R Lewin / Mikhail Kudryashev / ![]() Abstract: The naked mole-rat (Heterocephalus glaber) is a long-lived mammal with resistance to cancer and hypoxia, suggesting the evolution of robust proteostasis networks. The ribosome, central for protein ...The naked mole-rat (Heterocephalus glaber) is a long-lived mammal with resistance to cancer and hypoxia, suggesting the evolution of robust proteostasis networks. The ribosome, central for protein synthesis, is key to cellular stress responses and has an unusual feature: the 28S rRNA split; however, the details of its organization remain unknown. Here, we present high-resolution cryo-EM structures of the naked mole-rat 80S ribosome in four states of the elongation cycle. The structures reveal a conserved overall architecture and rRNA modification landscape compared to other mammals, and provide an atomic-level view of the distinct break in the 28S rRNA. This cleavage event, located in the D6 expansion segment, is structurally stabilized by a network of interactions with surrounding ribosomal proteins, maintaining the integrity of the large subunit. Our comparative analysis revealed that this compensatory network preserves a canonical architecture that is nearly indistinguishable from intact mouse and human ribosomes. These findings resolve the structural basis of this distinct cleavage, showing that it is a stable, integrated feature whose function is likely linked to more subtle regulatory mechanisms, rather than inducing major structural rearrangements. | ||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9t5c.cif.gz | 5.1 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| 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 |
|---|
-Related structure data
| Related structure data | ![]() 55100MC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
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) |
|---|---|
| #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 ... , 22 types, 22 molecules LALCLDLELFLHLJLMLPLSLTLULXLbLcLdLfLhLkLlLrLB
-60S ribosomal protein ... , 17 types, 17 molecules LGLILLLNLOLQLVLWLYLZLaLeLgLiLnLoLp
| #10: Protein | Mass: 30061.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6K8Y4 |
|---|---|
| #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 |
| #14: Protein | Mass: 24364.680 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6P3F5 |
| #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: A0AAX6PQU7 |
| #17: Protein | Mass: 23519.354 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6Q4S4 |
| #19: Protein | Mass: 21698.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5B890 |
| #24: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PVG0 |
| #25: Protein | Mass: 17825.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PSU9 |
| #27: Protein | Mass: 17303.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PRM3 |
| #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 |
| #29: Protein | Mass: 16648.613 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PG51 |
| #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: A0AAX6QD41 |
| #35: Protein | Mass: 13325.022 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6Q439 |
| #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: A0AAX6Q2T6 |
| #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 |
| #44: Protein | Mass: 10299.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6NNU1 |
-Ribosomal protein ... , 2 types, 2 molecules LRLj
| #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 |
|---|---|
| #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: A0AAX6PHM7 |
-Small ribosomal subunit protein ... , 10 types, 10 molecules SASBSCSDSFSKSLSOScSg
| #49: Protein | Mass: 32867.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6K1L6 |
|---|---|
| #50: Protein | Mass: 29942.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5C1K3 |
| #51: Protein | Mass: 31283.387 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6QEX7 |
| #52: Protein | Mass: 26715.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat)References: UniProt: G5AS76, DNA-(apurinic or apyrimidinic site) lyase |
| #54: Protein | Mass: 22913.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5B7K7 |
| #59: Protein | Mass: 18951.818 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6IZJ7 |
| #60: Protein | Mass: 18468.826 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6J0Q6 |
| #62: Protein | Mass: 16302.772 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0N8ESF7 |
| #76: Protein | Mass: 7855.052 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5B4M2 |
| #79: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6J231 |
-40S ribosomal protein ... , 20 types, 20 molecules SESGSHSISJSNSPSQSRSSSTSUSVSWSXSYSZSaSbSd
| #53: Protein | Mass: 29654.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0A0P6JF61 |
|---|---|
| #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 |
| #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: A0AAX6NNW6, protein-synthesizing GTPase |
| #57: Protein | Mass: 24263.387 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5ARV4 |
| #58: Protein | Mass: 22607.549 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6Q606 |
| #61: Protein | Mass: 17259.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PGK5 |
| #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: A0AAX6Q6L0 |
| #64: Protein | Mass: 16477.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PUA9 |
| #65: Protein | Mass: 15552.119 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PIW5 |
| #66: Protein | Mass: 17759.777 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PA22 |
| #67: Protein | Mass: 16117.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6QEV3 |
| #68: Protein | Mass: 13331.776 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6QEN2 |
| #69: Protein | Mass: 9169.388 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: G5C8F1 |
| #70: Protein | Mass: 14865.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PNI7 |
| #71: Protein | Mass: 15863.713 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6P1S3 |
| #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 |
| #73: Protein | Mass: 13776.224 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6PPX8 |
| #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: A0AAX6NNU4 |
| #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: A0AAX6NNV5 |
| #77: Protein | Mass: 6690.821 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Heterocephalus glaber (naked mole-rat) / References: UniProt: A0AAX6NS13 |
-Non-polymers , 3 types, 337 molecules 




| #81: Chemical | ChemComp-MG / #82: Chemical | #83: Water | ChemComp-HOH / | |
|---|
-Details
| Has ligand of interest | N |
|---|---|
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: 80S ribosome / Type: RIBOSOME / Entity ID: #1-#80 / Source: NATURAL |
|---|---|
| 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 |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| 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) |
-
Processing
| EM software |
| ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 |
Movie
Controller
About Yorodumi



Heterocephalus glaber (naked mole-rat)
Germany, 1items
Citation

PDBj

































FIELD EMISSION GUN
