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Open data
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Basic information
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| Title | EMCV IRES captured on mammalian 40S with initiator tRNA | |||||||||
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Sample |
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Keywords | EMCV IRES / 40S ribosome / 48S PIC / RIBOSOME | |||||||||
| 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 / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / gastrulation ...laminin receptor activity / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / translation regulator activity / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / gastrulation / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase / 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 / rhythmic process / positive regulation of canonical Wnt signaling pathway / 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 / cell differentiation / cytoplasmic translation / mitochondrial inner membrane / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / apoptotic process / centrosome / synapse / dendrite / perinuclear region of cytoplasm / nucleolus / Golgi apparatus / DNA binding / RNA binding / zinc ion binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() Encephalomyocarditis virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.6 Å | |||||||||
Authors | Das D / Hussain T | |||||||||
| Funding support | India, 1 items
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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
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Downloads & links
-EMDB archive
| Map data | emd_64644.map.gz | 230.2 MB | EMDB map data format | |
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| Header (meta data) | emd-64644-v30.xml emd-64644.xml | 57.5 KB 57.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_64644_fsc.xml | 13.3 KB | Display | FSC data file |
| Images | emd_64644.png | 54.2 KB | ||
| Filedesc metadata | emd-64644.cif.gz | 12.7 KB | ||
| Others | emd_64644_half_map_1.map.gz emd_64644_half_map_2.map.gz | 226.3 MB 226.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64644 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64644 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9uzkMC ![]() 9uzlC ![]() 9uzmC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_64644.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.17 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_64644_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_64644_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : EMCV IRES with 40S and initiator tRNA
+Supramolecule #1: EMCV IRES with 40S and initiator tRNA
+Macromolecule #1: 18S ribosomal RNA
+Macromolecule #36: Initiator tRNA
+Macromolecule #37: EMCV IRES
+Macromolecule #2: Small ribosomal subunit protein uS2
+Macromolecule #3: Small ribosomal subunit protein eS1
+Macromolecule #4: Small ribosomal subunit protein uS5
+Macromolecule #5: Small ribosomal subunit protein uS3
+Macromolecule #6: Small ribosomal subunit protein eS4
+Macromolecule #7: Small ribosomal subunit protein uS7
+Macromolecule #8: Small ribosomal subunit protein eS6
+Macromolecule #9: Small ribosomal subunit protein eS7
+Macromolecule #10: Small ribosomal subunit protein eS8
+Macromolecule #11: Small ribosomal subunit protein uS4
+Macromolecule #12: Small ribosomal subunit protein eS10
+Macromolecule #13: Small ribosomal subunit protein uS17
+Macromolecule #14: Small ribosomal subunit protein eS12
+Macromolecule #15: Small ribosomal subunit protein uS15
+Macromolecule #16: Ribosomal protein S14
+Macromolecule #17: Small ribosomal subunit protein uS19
+Macromolecule #18: Small ribosomal subunit protein uS9
+Macromolecule #19: Small ribosomal subunit protein eS17
+Macromolecule #20: Small ribosomal subunit protein uS13
+Macromolecule #21: Small ribosomal subunit protein eS19
+Macromolecule #22: Small ribosomal subunit protein uS10
+Macromolecule #23: Small ribosomal subunit protein eS21
+Macromolecule #24: Small ribosomal subunit protein uS8
+Macromolecule #25: Small ribosomal subunit protein uS12
+Macromolecule #26: 40S ribosomal protein S24
+Macromolecule #27: Small ribosomal subunit protein eS26
+Macromolecule #28: Small ribosomal subunit protein eS27
+Macromolecule #29: Small ribosomal subunit protein eS28
+Macromolecule #30: Small ribosomal subunit protein uS14
+Macromolecule #31: Ubiquitin-ribosomal protein eS31 fusion protein
+Macromolecule #32: Small ribosomal subunit protein RACK1
+Macromolecule #33: Small ribosomal subunit protein eS25
+Macromolecule #34: Small ribosomal subunit protein eS30
+Macromolecule #35: Small ribosomal subunit protein eS32
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 Details: 20mM HEPES, 150mM KOAc, 2mM MgCl2, 1mM DTT, 0.5mM Spermidine, 6mM GMP-PnP |
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| Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 70 sec. / Pretreatment - Atmosphere: OTHER |
| Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Temperature | Min: 77.0 K / Max: 83.0 K |
| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Number grids imaged: 6 / Number real images: 22549 / Average electron dose: 55.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.75 µm / Nominal defocus min: 1.25 µm / Nominal magnification: 36000 |
| Sample stage | Specimen holder model: OTHER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model |
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| Output model | ![]() PDB-9uzk: |
Movie
Controller
About Yorodumi




Keywords
Encephalomyocarditis virus
Authors
India, 1 items
Citation










Z (Sec.)
Y (Row.)
X (Col.)




































FIELD EMISSION GUN



