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Yorodumi- PDB-6d9j: Mammalian 80S ribosome with a double translocated CrPV-IRES, P-si... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6d9j | ||||||
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| Title | Mammalian 80S ribosome with a double translocated CrPV-IRES, P-sitetRNA and eRF1. | ||||||
Components |
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Keywords | RIBOSOME / mammalian / CrPV IRES | ||||||
| Function / homology | Function and homology informationSynthesis of diphthamide-EEF2 / translation at postsynapse / glial cell proliferation / skeletal muscle cell differentiation / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / gastrulation / translational elongation ...Synthesis of diphthamide-EEF2 / translation at postsynapse / glial cell proliferation / skeletal muscle cell differentiation / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / gastrulation / translational elongation / Peptide chain elongation / ubiquitin ligase inhibitor activity / response to ischemia / translation elongation factor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / skeletal muscle contraction / Protein methylation / cellular response to brain-derived neurotrophic factor stimulus / translation regulator activity / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / positive regulation of apoptotic signaling pathway / MDM2/MDM4 family protein binding / response to endoplasmic reticulum stress / 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 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) / response to hydrogen peroxide / maturation of SSU-rRNA / small-subunit processome / spindle / p53 binding / rRNA processing / cytosolic ribosome / actin filament binding / response to estradiol / regulation of translation / rhythmic process / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding / 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 / 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 / perikaryon / cell differentiation / cytoplasmic translation / tRNA binding / postsynapse / postsynaptic density / mitochondrial inner membrane / response to xenobiotic stimulus / rRNA binding / cadherin binding / ribosome / translation / structural constituent of ribosome / ribonucleoprotein complex / cell division / DNA repair / apoptotic process / mRNA binding / centrosome / GTPase activity / Neutrophil degranulation / nucleolus / dendrite / synapse / protein kinase binding / GTP binding / perinuclear region of cytoplasm / glutamatergic synapse / endoplasmic reticulum / DNA binding / DNA-templated transcription / RNA binding / extracellular exosome / extracellular region / zinc ion binding / membrane / metal ion binding / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)![]() ![]() Cricket paralysis virus | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||
Authors | Pisareva, V.P. / Pisarev, A.V. / Fernandez, I.S. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Elife / Year: 2018Title: Dual tRNA mimicry in the Cricket Paralysis Virus IRES uncovers an unexpected similarity with the Hepatitis C Virus IRES. Authors: Vera P Pisareva / Andrey V Pisarev / Israel S Fernández / ![]() Abstract: Co-opting the cellular machinery for protein production is a compulsory requirement for viruses. The Cricket Paralysis Virus employs an Internal Ribosomal Entry Site (CrPV-IRES) to express its ...Co-opting the cellular machinery for protein production is a compulsory requirement for viruses. The Cricket Paralysis Virus employs an Internal Ribosomal Entry Site (CrPV-IRES) to express its structural genes in the late stage of infection. Ribosome hijacking is achieved by a sophisticated use of molecular mimicry to tRNA and mRNA, employed to manipulate intrinsically dynamic components of the ribosome. Binding and translocation through the ribosome is required for this IRES to initiate translation. We report two structures, solved by single particle electron cryo-microscopy (cryoEM), of a double translocated CrPV-IRES with aminoacyl-tRNA in the peptidyl site (P site) of the ribosome. CrPV-IRES adopts a previously unseen conformation, mimicking the acceptor stem of a canonical E site tRNA. The structures suggest a mechanism for the positioning of the first aminoacyl-tRNA shared with the distantly related Hepatitis C Virus IRES. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6d9j.cif.gz | 5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6d9j.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 6d9j.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d9/6d9j ftp://data.pdbj.org/pub/pdb/validation_reports/d9/6d9j | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 7836MC ![]() 7834C ![]() 6d90C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Ribosomal protein ... , 18 types, 18 molecules ACJNVejtEEGGKKMMOORRXXYYddgg
| #1: Protein | Mass: 28088.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 44232.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 20288.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 24207.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #30: Protein | Mass: 15898.932 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 21295.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #53: Protein | Mass: 31146.607 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 22913.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #59: Protein | Mass: 22641.564 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #61: Protein | Mass: 18468.826 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #63: Protein | Mass: 17259.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #66: Protein | Mass: 19213.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #72: Protein | Mass: 14865.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #73: Protein | Mass: 15784.549 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: Protein | Mass: 7855.052 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #81: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Protein , 41 types, 41 molecules BFGOQRSTUWXYabcdfhklmprsKBBDDFFLLPP...
-Large ribosomal subunit protein ... , 5 types, 5 molecules DMPgo
| #4: Protein | Mass: 34479.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #12: Protein | Mass: 21950.322 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 21741.596 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #32: Protein | Mass: 14210.088 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #40: Protein | Mass: 12476.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-60S ribosomal protein ... , 6 types, 6 molecules EHILZi
| #5: Protein | Mass: 33028.336 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 21871.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 24643.057 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 24331.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 15835.831 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: Protein | Mass: 12263.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 1 types, 1 molecules n
| #39: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-RNA chain , 6 types, 6 molecules 578234
| #45: RNA chain | Mass: 1164731.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #46: RNA chain | Mass: 38385.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: RNA chain | Mass: 48545.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: RNA chain | Mass: 547733.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #83: RNA chain | Mass: 28094.645 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: RNA was prepared by in vitro transcription with T7 RNA polymerase Source: (synth.) ![]() |
| #85: RNA chain | Mass: 60789.762 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: RNA was prepared by in vitro transcription with T7 RNA polymerase Source: (synth.) Cricket paralysis virus / References: GenBank: 8895506 |
-40S ribosomal protein ... , 8 types, 8 molecules CCHHIIJJNNZZccff
| #51: Protein | Mass: 30002.061 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #56: Protein | Mass: 28751.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 22168.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 24003.012 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #62: Protein | Mass: 14538.987 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #74: Protein | Mass: 15548.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #77: Protein | Mass: 9480.186 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #80: Protein | Mass: 14498.884 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 6 molecules 


| #86: Chemical | ChemComp-ZN / #87: Chemical | |
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-Details
| Has protein modification | N |
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-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: Mammalian 80S ribosome in complex with translocated CrPV IRES, P-site tRNA and eEF2 Type: RIBOSOME Details: Mammalian 80S ribosome in complex with translocated CrPV IRES, P-site tRNA and eRF1 Entity ID: #1-#85 / Source: NATURAL |
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| Molecular weight | Value: 5 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD |
| 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: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 75654 / Symmetry type: POINT |
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About Yorodumi



Homo sapiens (human)

Cricket paralysis virus
United States, 1items
Citation
UCSF Chimera












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