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Yorodumi- PDB-9q2m: Rabbit ribosomal 80S elongation complex with eEF2, partial P site... -
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Basic information
| Entry | Database: PDB / ID: 9q2m | |||||||||||||||||||||||||||
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| Title | Rabbit ribosomal 80S elongation complex with eEF2, partial P site Ala-tRNA, E site Ala-tRNA on NediV ORF | |||||||||||||||||||||||||||
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Keywords | RIBOSOME / IRES / Translation / Initiation | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationSynthesis of diphthamide-EEF2 / translation at postsynapse / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / skeletal muscle cell differentiation / translational elongation / Peptide chain elongation / ubiquitin ligase inhibitor activity ...Synthesis of diphthamide-EEF2 / translation at postsynapse / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / skeletal muscle cell differentiation / translational elongation / Peptide chain elongation / ubiquitin ligase inhibitor activity / glial cell proliferation / translation elongation factor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / skeletal muscle contraction / protein-RNA complex assembly / cellular response to brain-derived neurotrophic factor stimulus / Protein methylation / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / response to ischemia / MDM2/MDM4 family protein binding / response to endoplasmic reticulum stress / positive regulation of apoptotic signaling pathway / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / ribosomal large subunit biogenesis / positive regulation of translation / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to hydrogen peroxide / cytosolic ribosome / maturation of SSU-rRNA / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / small-subunit processome / spindle / cytoplasmic ribonucleoprotein granule / p53 binding / rRNA processing / actin filament binding / response to estradiol / regulation of translation / heparin binding / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / 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 / secretory granule lumen / killing of cells of another organism / defense response to Gram-negative bacterium / cytosolic large ribosomal subunit / ficolin-1-rich granule lumen / response to ethanol / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cell differentiation / cytoplasmic translation / tRNA binding / postsynapse / mitochondrial inner membrane / postsynaptic density / negative regulation of translation / rRNA binding / response to xenobiotic stimulus / structural constituent of ribosome / cadherin binding / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / GTPase activity / centrosome / apoptotic process / Neutrophil degranulation / nucleolus / synapse / protein kinase binding / GTP binding / glutamatergic synapse / endoplasmic reticulum / DNA-templated transcription / DNA binding / RNA binding / extracellular exosome / extracellular region / zinc ion binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() Nedicistrovirus TFN-2012 | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 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. | |||||||||||||||||||||||||||
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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 | 9q2m.cif.gz | 5.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q2m.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9q2m.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q2/9q2m ftp://data.pdbj.org/pub/pdb/validation_reports/q2/9q2m | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72168MC ![]() 9q1qC ![]() 9q1sC ![]() 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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Components
+60S ribosomal protein ... , 25 types, 25 molecules RABCDEFHJMNPTYZacdghijlpr
-Protein , 11 types, 11 molecules WAAVVaaISbostEF
| #2: Protein | Mass: 12267.337 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: Protein | Mass: 24361.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 9124.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 11645.794 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 24511.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 20827.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #60: Protein | Mass: 12093.424 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #73: Protein | Mass: 12198.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #76: Protein | Mass: 21521.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #77: Protein | Mass: 16561.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #81: Protein | Mass: 95260.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P13639, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
-RNA chain , 7 types, 7 molecules 95781PTET
| #3: RNA chain | Mass: 539041.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #78: RNA chain | Mass: 1147859.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #79: RNA chain | Mass: 38385.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #80: RNA chain | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #82: RNA chain | Mass: 3426.106 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Nedicistrovirus TFN-2012 |
| #83: RNA chain | Mass: 3483.114 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
| #84: RNA chain | Mass: 24475.549 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
+40S ribosomal protein ... , 21 types, 21 molecules BBCCEEGGIIJJNNWWXXYYbbDDKKMMRRSSUUZZccddff
-Small ribosomal subunit protein ... , 8 types, 8 molecules HHLLOOeeFFPPQQTT
| #9: Protein | Mass: 21629.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #12: Protein | Mass: 17586.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 14544.659 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 6512.737 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: Protein | Mass: 21525.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 13668.165 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #27: Protein | Mass: 15875.610 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #30: Protein | Mass: 15611.003 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Large ribosomal subunit protein ... , 11 types, 11 molecules GLOQUVXefkm
| #42: Protein | Mass: 27351.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #46: Protein | Mass: 24200.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 23144.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #51: Protein | Mass: 21568.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: Protein | Mass: 11495.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 14761.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #56: Protein | Mass: 13727.181 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #63: Protein | Mass: 15022.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #64: Protein | Mass: 12449.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #69: Protein | Mass: 8107.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #71: Protein | Mass: 6199.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 1 types, 1 molecules n
| #72: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 214 molecules 


| #85: Chemical | ChemComp-MG / #86: Chemical | ChemComp-ZN / |
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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: Rabbit ribosomal 80S elongation complex with eEF2, partial P site Ala-tRNA, E site Ala-tRNA on NediV ORF Type: RIBOSOME Entity ID: #1-#18, #20-#33, #36, #38-#43, #45-#49, #52-#54, #56-#58, #60-#64, #66-#67, #69-#70, #72, #75-#77, #81-#82, #19, #85 Source: MULTIPLE SOURCES |
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| 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: 3500 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: NONE | ||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 34773 / Symmetry type: POINT |
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Nedicistrovirus TFN-2012
United States, 4items
Citation








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FIELD EMISSION GUN