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Open data
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Basic information
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| Title | NediV IRES (P site) in complex with Rabbit 80S ribosome | |||||||||||||||
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Keywords | Ribosome / IRES / Translation / Initiation | |||||||||||||||
| Function / homology | Function and homology information90S preribosome / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / protein-RNA complex assembly / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase ...90S preribosome / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / protein-RNA complex assembly / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 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 / regulation of translation / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit / ribosomal small subunit assembly / 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 / killing of cells of another organism / cytosolic large ribosomal subunit / defense response to Gram-negative bacterium / cell differentiation / cytoplasmic translation / tRNA binding / mitochondrial inner membrane / negative regulation of translation / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / apoptotic process / centrosome / synapse / nucleolus / endoplasmic reticulum / DNA binding / RNA binding / zinc ion binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||||||||
| Biological species | Nedicistrovirus TFN-2012 / ![]() | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||||||||
Authors | De S / Altomare CG / Abaeva IS / Dadhwal P / Garg P / Acosta-Reyes F / Brown ZP / Pestova TV / Hellen CUT / Frank J | |||||||||||||||
| Funding support | United States, 4 items
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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
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Downloads & links
-EMDB archive
| Map data | emd_72137.map.gz | 31.9 MB | EMDB map data format | |
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| Header (meta data) | emd-72137-v30.xml emd-72137.xml | 99.7 KB 99.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_72137_fsc.xml | 7.5 KB | Display | FSC data file |
| Images | emd_72137.png | 189.4 KB | ||
| Filedesc metadata | emd-72137.cif.gz | 18.7 KB | ||
| Others | emd_72137_additional_1.map.gz emd_72137_half_map_1.map.gz emd_72137_half_map_2.map.gz | 55.4 MB 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72137 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72137 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9q1sMC ![]() 9q1qC ![]() 9q2mC ![]() 9q2pC ![]() 9q2tC 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_72137.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Voxel size | X=Y=Z: 1.25 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_72137_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_72137_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_72137_half_map_2.map | ||||||||||||
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Sample components
+Entire : Rabbit 80S ribosome in complex with NediV IRES
+Supramolecule #1: Rabbit 80S ribosome in complex with NediV IRES
+Macromolecule #1: 18S rRNA
+Macromolecule #21: 28S ribosomal RNA
+Macromolecule #22: 5S rRNA
+Macromolecule #23: 5.8S rRNA
+Macromolecule #47: NediV IRES
+Macromolecule #2: 60S ribosomal protein L8
+Macromolecule #3: 60S ribosomal protein L3
+Macromolecule #4: 60S ribosomal protein L4
+Macromolecule #5: Large ribosomal subunit protein eL6
+Macromolecule #6: Large ribosomal subunit protein eL8
+Macromolecule #7: 60S ribosomal protein L9
+Macromolecule #8: Ribosomal protein L10
+Macromolecule #9: 60S ribosomal protein L11
+Macromolecule #10: Large ribosomal subunit protein eL13
+Macromolecule #11: 60S ribosomal protein L15
+Macromolecule #12: Large ribosomal subunit protein uL13
+Macromolecule #13: 60S ribosomal protein L19
+Macromolecule #14: Large ribosomal subunit protein uL14
+Macromolecule #15: Large ribosomal subunit protein eL24
+Macromolecule #16: Large ribosomal subunit protein uL23
+Macromolecule #17: 60S ribosomal protein L26
+Macromolecule #18: 60S ribosomal protein L27a
+Macromolecule #19: Large ribosomal subunit protein eL29
+Macromolecule #20: Large ribosomal subunit protein eL32
+Macromolecule #24: 60S ribosomal protein L5
+Macromolecule #25: 60S ribosomal protein L7
+Macromolecule #26: 60S ribosomal protein L14
+Macromolecule #27: 60S ribosomal protein L17
+Macromolecule #28: Large ribosomal subunit protein eL18
+Macromolecule #29: eL20
+Macromolecule #30: 60S ribosomal protein L21
+Macromolecule #31: eL22
+Macromolecule #32: 60S ribosomal protein L27
+Macromolecule #33: 60S ribosomal protein L30
+Macromolecule #34: 60S ribosomal protein L31
+Macromolecule #35: Large ribosomal subunit protein eL33
+Macromolecule #36: 60S ribosomal protein L34
+Macromolecule #37: 60S ribosomal protein L35
+Macromolecule #38: 60S ribosomal protein L36
+Macromolecule #39: 60S ribosomal protein L37
+Macromolecule #40: Large ribosomal subunit protein eL38
+Macromolecule #41: 60S ribosomal protein L39
+Macromolecule #42: Large ribosomal subunit protein eL40
+Macromolecule #43: eL41
+Macromolecule #44: eL42
+Macromolecule #45: 60S ribosomal protein L37a
+Macromolecule #46: 60S ribosomal protein L28
+Macromolecule #48: eL1
+Macromolecule #49: 40S_SA_C domain-containing protein
+Macromolecule #50: 40S ribosomal protein S3a
+Macromolecule #51: 40S ribosomal protein S2
+Macromolecule #52: 40S ribosomal protein S4
+Macromolecule #53: Small ribosomal subunit protein eS6
+Macromolecule #54: Small ribosomal subunit protein eS7
+Macromolecule #55: 40S ribosomal protein S8
+Macromolecule #56: Small ribosomal subunit protein uS4
+Macromolecule #57: Small ribosomal subunit protein uS17
+Macromolecule #58: 40S ribosomal protein S13
+Macromolecule #59: Small ribosomal subunit protein uS11
+Macromolecule #60: eS21
+Macromolecule #61: 40S ribosomal protein S15a
+Macromolecule #62: 40S ribosomal protein S23
+Macromolecule #63: 40S ribosomal protein S24
+Macromolecule #64: eS26
+Macromolecule #65: 40S ribosomal protein S27
+Macromolecule #66: Small ribosomal subunit protein eS30
+Macromolecule #67: Small ribosomal subunit protein uS3
+Macromolecule #68: Small ribosomal subunit protein uS7
+Macromolecule #69: Small ribosomal subunit protein eS10
+Macromolecule #70: Small ribosomal subunit protein uS19
+Macromolecule #71: Small ribosomal subunit protein uS9
+Macromolecule #72: 40S ribosomal protein S17
+Macromolecule #73: 40S ribosomal protein S18
+Macromolecule #74: Small ribosomal subunit protein eS19
+Macromolecule #75: uS10
+Macromolecule #76: 40S ribosomal protein S25
+Macromolecule #77: 40S ribosomal protein S28
+Macromolecule #78: 40S ribosomal protein S29
+Macromolecule #79: MAGNESIUM ION
+Macromolecule #80: ZINC ION
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI POLARA 300 |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 64.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Nedicistrovirus TFN-2012
Authors
United States, 4 items
Citation
















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












































Processing
FIELD EMISSION GUN


