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Open data
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Basic information
| Entry | Database: PDB / ID: 9uzk | ||||||||||||||||||||||||
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| Title | EMCV IRES captured on mammalian 40S with initiator tRNA | ||||||||||||||||||||||||
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Keywords | RIBOSOME / EMCV IRES / 40S ribosome / 48S PIC | ||||||||||||||||||||||||
| Function / homology | Function and homology informationlaminin receptor activity / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / translation regulator activity / gastrulation / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding ...laminin receptor activity / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / translation regulator activity / gastrulation / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / positive regulation of apoptotic signaling pathway / DNA-(apurinic or apyrimidinic site) lyase / cytosolic ribosome / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / spindle / rRNA processing / rhythmic process / regulation of translation / ribosomal small subunit assembly / virus receptor activity / ribosome binding / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / perikaryon / cytoplasmic translation / cell differentiation / mitochondrial inner membrane / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / apoptotic process / centrosome / dendrite / synapse / nucleolus / perinuclear region of cytoplasm / DNA-templated transcription / DNA binding / RNA binding / zinc ion binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Encephalomyocarditis virus![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å | ||||||||||||||||||||||||
Authors | Das, D. / Hussain, T. | ||||||||||||||||||||||||
| Funding support | India, 1items
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Citation | Journal: Elife / Year: 2026Title: Structural insights into the recruitment of viral type 2 IRES to ribosomal preinitiation complex for protein synthesis. Authors: Deepakash Das / Tanweer Hussain / ![]() Abstract: Picornaviruses employ internal ribosome entry sites (IRESs) in their genomic RNA to hijack the host's translational machinery. The picornavirus, encephalomyocarditis virus, employs a type 2 IRES ...Picornaviruses employ internal ribosome entry sites (IRESs) in their genomic RNA to hijack the host's translational machinery. The picornavirus, encephalomyocarditis virus, employs a type 2 IRES present in its 5' untranslated region (5'UTR) and requires 43S ribosomal preinitiation complex (PIC), the central domain of eukaryotic initiation factor (eIF) 4G, eIF4A, and an essential ITAF (IRES trans-acting factor)-polypyrimidine tract binding protein 1 (PTB1) to form 48S PIC. In this study, we have used cryo-electron microscopy (cryo-EM) to determine the structure of encephalomyocarditis virus (EMCV) IRES-bound mammalian 48S PIC in a scanning-arrested closed state at the start codon. The EMCV IRES domains contact initiator tRNA (tRNA) and 40S head at the inter-subunit interface, which reveals an altogether unique mechanism used by viruses to capture host translational machinery for its protein synthesis. The tRNA is held away from the 40S body in contrast to canonical cap-dependent translation while the domain I apical region of EMCV IRES mimics 28S rRNA of 60S to interact with 40S ribosomal head proteins uS13 and uS19. The structural analysis accounts for numerous previously reported biochemical studies on type 2 IRES and shows how type 2 IRES interacts with 43S PIC to form 48S PIC. This study provides mechanistic insights for understanding EMCV IRES-mediated translation initiation, which could be extrapolated to other IRESs sharing similar motifs and factor requirements, including type 1 viral IRESs. #1: Journal: Elife / Year: 2026Title: Structural insights into the recruitment of viral Type 2 IRES to ribosomal preinitiation complex for protein synthesis Authors: Das, D. / Hussain, T. | ||||||||||||||||||||||||
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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 | 9uzk.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9uzk.ent.gz | 1.4 MB | Display | PDB format |
| PDBx/mmJSON format | 9uzk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/9uzk ftp://data.pdbj.org/pub/pdb/validation_reports/uz/9uzk | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 64644MC ![]() 9uzlC ![]() 9uzmC 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 , 3 types, 3 molecules 2yz
| #1: RNA chain | Mass: 600900.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #36: RNA chain | Mass: 24231.510 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: RNA chain | Mass: 29887.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Encephalomyocarditis virus / Production host: ![]() |
+Small ribosomal subunit protein ... , 31 types, 31 molecules CDEFGHIJKLMNOPRSTUVWXYZbcdeghil
-Protein , 3 types, 3 molecules Qaf
| #16: Protein | Mass: 18133.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #26: Protein | Mass: 14575.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #31: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Details
| Has protein modification | Y |
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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: EMCV IRES with 40S and initiator tRNA / Type: RIBOSOME Details: EMCV IRES captured in 48S PIC using affinity-based pull-down from rabbit reticulocyte lysate Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 Details: 20mM HEPES, 150mM KOAc, 2mM MgCl2, 1mM DTT, 0.5mM Spermidine, 6mM GMP-PnP |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 289 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 36000 X / Nominal defocus max: 2750 nm / Nominal defocus min: 1250 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: OTHER / Temperature (max): 83 K / Temperature (min): 77 K |
| Image recording | Electron dose: 55 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 6 / Num. of real images: 22549 |
| Image scans | Width: 3838 / Height: 3710 / Movie frames/image: 20 |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55231 / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Atomic model building | 3D fitting-ID: 1
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Movie
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About Yorodumi




Encephalomyocarditis virus

India, 1items
Citation




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FIELD EMISSION GUN

