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Open data
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Basic information
| Entry | Database: PDB / ID: 9q1s | |||||||||||||||||||||||||||
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| Title | NediV IRES (P site) in complex with Rabbit 80S ribosome | |||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / IRES / Translation / Initiation | |||||||||||||||||||||||||||
| Function / homology | Function and homology information90S preribosome / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / protein-RNA complex assembly / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase ...90S preribosome / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / protein-RNA complex assembly / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase / ribosomal large subunit biogenesis / 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) / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA / small-subunit processome / spindle / rRNA processing / regulation of translation / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit / ribosomal small subunit assembly / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / killing of cells of another organism / cytosolic large ribosomal subunit / defense response to Gram-negative bacterium / cell differentiation / cytoplasmic translation / tRNA binding / mitochondrial inner membrane / negative regulation of translation / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / apoptotic process / centrosome / synapse / nucleolus / endoplasmic reticulum / DNA binding / RNA binding / zinc ion binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Nedicistrovirus TFN-2012![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||||||||||||||||||||
Authors | De, S. / Altomare, C.G. / Abaeva, I.S. / Dadhwal, P. / Garg, P. / Acosta-Reyes, F. / Brown, Z.P. / Pestova, T.V. / Hellen, C.U.T. / Frank, J. | |||||||||||||||||||||||||||
| Funding support | United States, 4items
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Citation | Journal: Nucleic Acids Res / Year: 2026Title: Structural studies of nedicistrovirus IRES-driven, initiation factor-independent translation shed light on key steps of eukaryotic translation elongation. Authors: Swastik De / Clara G Altomare / Irina S Abaeva / Prikshat Dadhwal / Priyanka Garg / Francisco Acosta-Reyes / Zuben P Brown / Tatyana V Pestova / Christopher U T Hellen / Joachim Frank / ![]() Abstract: We utilized the nedicistrovirus (NediV) intergenic region (IGR) internal ribosomal entry site (IRES)-mediated, initiation factor-independent translation initiation system and determined high- ...We utilized the nedicistrovirus (NediV) intergenic region (IGR) internal ribosomal entry site (IRES)-mediated, initiation factor-independent translation initiation system and determined high-resolution structures of 80S ribosome complexes with the NediV IRES in various functional states, including binary complexes, aminoacyl-transfer RNA (tRNA)-bound complexes, and complexes with elongation factor eEF2. In binary complexes, the NediV IRES primarily occupies the ribosomal P site, exhibiting conformational flexibility and engaging the ribosome at multiple interaction sites. Upon translocation, the IRES undergoes structural rearrangements, including destabilization of its PKI domain, facilitating the transition to canonical elongation. Crucially, we captured an eEF2-bound complex, along with an eEF1A-bound failed decoding complex featuring a mismatched tRNA, the latter representing the first instance of a canonical elongation complex visualized in the presence of a natural, hydrolysable nucleotide and without the addition of any trapping agents. These findings provide a comprehensive structural overview of IGR IRES-mediated translation initiation and its transition to elongation, revealing key mechanistic details of viral translation and proofreading. | |||||||||||||||||||||||||||
| History |
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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 | 9q1s.cif.gz | 4.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q1s.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9q1s.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q1/9q1s ftp://data.pdbj.org/pub/pdb/validation_reports/q1/9q1s | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72137MC ![]() 9q1qC ![]() 9q2mC ![]() 9q2pC ![]() 9q2tC 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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| 1 |
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Components
-RNA chain , 5 types, 5 molecules 95781
| #1: RNA chain | Mass: 539096.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #21: RNA chain | Mass: 1148115.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #22: RNA chain | Mass: 38385.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: RNA chain | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: RNA chain | Mass: 53498.551 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nedicistrovirus TFN-2012 / Production host: ![]() |
+60S ribosomal protein ... , 24 types, 24 molecules ABCHJNRYaDFMPTZcdghijlpr
-Large ribosomal subunit protein ... , 13 types, 13 molecules EGLOVWXbeQfkm
| #5: Protein | Mass: 28818.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: Protein | Mass: 27351.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 24200.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 23144.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 14761.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 11063.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 13727.181 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 13401.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 15022.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #28: Protein | Mass: 21568.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 12449.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #40: Protein | Mass: 8107.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 6199.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 8 types, 8 molecules ISUoKAAVVaa
| #8: Protein | Mass: 24511.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #29: Protein | Mass: 20827.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #31: Protein | Mass: 11495.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 12198.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: Protein | Mass: 15205.939 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 24361.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #60: Protein | Mass: 9124.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #64: Protein | Mass: 11645.794 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 2 types, 2 molecules nUU
| #43: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #75: Protein/peptide | Mass: 5686.793 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-40S ribosomal protein ... , 14 types, 14 molecules BBCCEEIINNWWXXYYbbRRSSZZccdd
| #50: Protein | Mass: 24759.145 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #51: Protein | Mass: 24441.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 29523.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 24003.012 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 17057.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #61: Protein | Mass: 14734.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #62: Protein | Mass: 15626.392 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #63: Protein | Mass: 14432.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #65: Protein | Mass: 9348.990 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #72: Protein | Mass: 15250.714 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #73: Protein | Mass: 16898.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #76: Protein | Mass: 8526.119 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #77: Protein | Mass: 7007.069 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: Protein | Mass: 6559.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 12 types, 12 molecules GGHHJJLLOOeeDDFFKKPPQQTT
| #53: Protein | Mass: 25900.691 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #54: Protein | Mass: 21629.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #56: Protein | Mass: 20892.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 17586.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #59: Protein | Mass: 14544.659 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #66: Protein | Mass: 6512.737 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #67: Protein | Mass: 23349.508 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: G1TNM3, DNA-(apurinic or apyrimidinic site) lyase |
| #68: Protein | Mass: 21525.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #69: Protein | Mass: 9384.134 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #70: Protein | Mass: 15115.795 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #71: Protein | Mass: 15451.144 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #74: Protein | Mass: 15611.003 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 213 molecules 


| #79: Chemical | ChemComp-MG / #80: Chemical | ChemComp-ZN / |
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-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: Rabbit 80S ribosome in complex with NediV IRES / Type: RIBOSOME / Entity ID: #1-#46, #48-#78 / Source: RECOMBINANT |
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| Source (natural) | Organism: Nedicistrovirus TFN-2012 |
| Source (recombinant) | Organism: ![]() |
| 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: Tecnai Polara / Image courtesy: FEI Company |
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| Microscopy | Model: FEI POLARA 300 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 64 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 264326 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Nedicistrovirus TFN-2012

United States, 4items
Citation








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FIELD EMISSION GUN