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Yorodumi- PDB-9q2p: Rabbit ribosomal 80S elongation complex with eEF1A, A*/T Ala-tRNA... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9q2p | ||||||||||||||||||||||||||||||
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| Title | Rabbit ribosomal 80S elongation complex with eEF1A, A*/T Ala-tRNA, P site Ala-tRNA, E site Ala-tRNA on NediV ORF | ||||||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / IRES / Translation / Initiation | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationguanyl nucleotide binding / protein-RNA complex assembly / kinase activator activity / regulation of translation involved in cellular response to UV / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator / translational elongation / translation elongation factor activity / ubiquitin ligase inhibitor activity ...guanyl nucleotide binding / protein-RNA complex assembly / kinase activator activity / regulation of translation involved in cellular response to UV / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator / translational elongation / translation elongation factor activity / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / negative regulation of ubiquitin-dependent protein catabolic process / translation regulator activity / ribosomal small subunit export from nucleus / rough endoplasmic reticulum / positive regulation of apoptotic signaling pathway / MDM2/MDM4 family protein binding / cellular response to epidermal growth factor stimulus / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / DNA damage response, signal transduction by p53 class mediator / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / positive regulation of translation / small-subunit processome / cellular response to gamma radiation / spindle / cytoplasmic ribonucleoprotein granule / mRNA 5'-UTR binding / transcription coactivator binding / rRNA processing / cytosolic ribosome / glucose homeostasis / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / perikaryon / cytoplasmic translation / postsynaptic density / protein stabilization / rRNA binding / negative regulation of translation / mitochondrial inner membrane / ribonucleoprotein complex / structural constituent of ribosome / ribosome / translation / mRNA binding / ubiquitin protein ligase binding / centrosome / GTPase activity / positive regulation of cell population proliferation / nucleolus / dendrite / GTP binding / synapse / negative regulation of transcription by RNA polymerase II / perinuclear region of cytoplasm / endoplasmic reticulum / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm 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. | ||||||||||||||||||||||||||||||
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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 | 9q2p.cif.gz | 8.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q2p.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9q2p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q2/9q2p ftp://data.pdbj.org/pub/pdb/validation_reports/q2/9q2p | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72171MC ![]() 9q1qC ![]() 9q1sC ![]() 9q2mC ![]() 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
-RNA chain , 7 types, 8 molecules 723589AT1
| #1: RNA chain | Mass: 38385.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() | ||||||||||
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| #46: RNA chain | Mass: 24130.342 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() #47: RNA chain | | Mass: 1147900.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() #48: RNA chain | | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() #49: RNA chain | | Mass: 547734.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() #83: RNA chain | | Mass: 24475.549 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polyribonucleotide / Source: (natural) ![]() #85: RNA chain | | Mass: 4695.866 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Nedicistrovirus TFN-2012 |
+60S ribosomal protein ... , 26 types, 26 molecules ABCDEFHJMNPRSTYZacdghijlpr
-Large ribosomal subunit protein ... , 11 types, 11 molecules GLOQUVXefkm
| #8: Protein | Mass: 27351.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
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| #12: Protein | Mass: 24200.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #15: Protein | Mass: 23144.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #17: Protein | Mass: 21568.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #21: Protein | Mass: 11495.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #22: Protein | Mass: 14761.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #24: Protein | Mass: 13727.181 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #31: Protein | Mass: 15022.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #32: Protein | Mass: 12449.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #37: Protein | Mass: 8107.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #39: Protein | Mass: 6199.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
-Protein , 11 types, 11 molecules IWbostAAVVaaggEF
| #10: Protein | Mass: 24511.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
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| #23: Protein | Mass: 12267.337 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #28: Protein | Mass: 12093.424 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #41: Protein | Mass: 12198.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #44: Protein | Mass: 21521.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #45: Protein | Mass: 16561.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #50: Protein | Mass: 24361.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #71: Protein | Mass: 9124.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #76: Protein | Mass: 11645.794 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #82: Protein | Mass: 34669.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #84: Protein | Mass: 48247.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() References: UniProt: P68105, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
-Protein/peptide , 1 types, 1 molecules n
| #40: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
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+40S ribosomal protein ... , 21 types, 21 molecules BBCCDDEEGGIIJJKKMMNNRRSSUUWWXXYYZZbbccddff
-Small ribosomal subunit protein ... , 8 types, 8 molecules FFHHLLOOPPQQTTee
| #55: Protein | Mass: 21525.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
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| #57: Protein | Mass: 21629.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #61: Protein | Mass: 17586.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #64: Protein | Mass: 14544.659 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #65: Protein | Mass: 15115.795 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #66: Protein | Mass: 16032.804 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #69: Protein | Mass: 15611.003 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
| #80: Protein | Mass: 6512.737 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: polypeptide(L) / Source: (natural) ![]() |
-Non-polymers , 3 types, 285 molecules 




| #86: Chemical | ChemComp-MG / #87: Chemical | ChemComp-ZN / #88: Chemical | ChemComp-GTP / | |
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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: NediV IRES (P-site) in complex with Rabbit 80S / Type: RIBOSOME Entity ID: #2, #4-#9, #11-#15, #18-#21, #23-#26, #28-#32, #34-#35, #37-#38, #40, #43-#46, #50-#75, #77-#78, #80, #82-#83, #85 Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | 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: 3500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 58 e/Å2 / Film or detector model: GATAN K2 BASE (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 107135 / Symmetry type: POINT |
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About Yorodumi




Nedicistrovirus TFN-2012
United States, 4items
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FIELD EMISSION GUN