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Open data
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Basic information
| Entry | Database: PDB / ID: 9q3e | |||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of RotavirusA NSP1-ELOB-ELOC-CUL3 | |||||||||||||||||||||||||||||||||
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Keywords | VIRAL PROTEIN / Viral effector / E3 ligase / NSP1 / CUL3 | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationpositive regulation of mitotic cell cycle phase transition / POZ domain binding / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity / host cytoskeleton / negative regulation of Rho protein signal transduction / embryonic cleavage / polar microtubule / anaphase-promoting complex-dependent catabolic process / nuclear protein quality control by the ubiquitin-proteasome system / regulation protein catabolic process at postsynapse ...positive regulation of mitotic cell cycle phase transition / POZ domain binding / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity / host cytoskeleton / negative regulation of Rho protein signal transduction / embryonic cleavage / polar microtubule / anaphase-promoting complex-dependent catabolic process / nuclear protein quality control by the ubiquitin-proteasome system / regulation protein catabolic process at postsynapse / COPII vesicle coat assembly / cell projection organization / RHOBTB3 ATPase cycle / stem cell division / target-directed miRNA degradation / positive regulation of mitotic metaphase/anaphase transition / elongin complex / Notch binding / stress fiber assembly / RHOBTB1 GTPase cycle / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / negative regulation of DNA-templated DNA replication / Cul3-RING ubiquitin ligase complex / negative regulation of type I interferon production / positive regulation of cytokinesis / ubiquitin ligase complex scaffold activity / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / protein monoubiquitination / mitotic metaphase chromosome alignment / endoplasmic reticulum to Golgi vesicle-mediated transport / Tat-mediated elongation of the HIV-1 transcript / RHOBTB2 GTPase cycle / Formation of HIV-1 elongation complex containing HIV-1 Tat / sperm flagellum / Formation of HIV elongation complex in the absence of HIV Tat / protein autoubiquitination / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / kidney development / intrinsic apoptotic signaling pathway / ribosome-associated ubiquitin-dependent protein catabolic process / protein K48-linked ubiquitination / RNA Polymerase II Pre-transcription Events / regulation of cellular response to insulin stimulus / positive regulation of TORC1 signaling / gene expression / integrin-mediated signaling pathway / cellular response to amino acid stimulus / cyclin binding / positive regulation of protein ubiquitination / transcription corepressor binding / TP53 Regulates Transcription of DNA Repair Genes / G1/S transition of mitotic cell cycle / transcription initiation at RNA polymerase II promoter / protein destabilization / Degradation of DVL / transcription elongation by RNA polymerase II / Hedgehog 'on' state / Inactivation of CSF3 (G-CSF) signaling / Vif-mediated degradation of APOBEC3G / mitotic spindle / Evasion by RSV of host interferon responses / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / SPOP-mediated proteasomal degradation of PD-L1(CD274) / spindle pole / Regulation of expression of SLITs and ROBOs / protein polyubiquitination / microtubule cytoskeleton / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / Regulation of RAS by GAPs / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / ubiquitin protein ligase activity / KEAP1-NFE2L2 pathway / cell migration / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / protein-containing complex assembly / cellular response to oxidative stress / ubiquitin-dependent protein catabolic process / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / Potential therapeutics for SARS / symbiont-mediated suppression of host NF-kappaB cascade / proteasome-mediated ubiquitin-dependent protein catabolic process / host cell cytoplasm / protein-macromolecule adaptor activity / postsynapse / protein ubiquitination / inflammatory response / ubiquitin protein ligase binding / centrosome / positive regulation of cell population proliferation / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / glutamatergic synapse Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | Rotavirus A Homo sapiens (human) | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||||||||||||||
Authors | Baek, K. / Glassman, C.R. / Fischer, E.S. | |||||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: Science / Year: 2026Title: Virome-wide ubiquitin ligase discovery reveals diverse mechanisms of immune evasion. Authors: Caleb R Glassman / Kheewoong Baek / Gaopeng Hou / Qiru Zeng / Christopher Nardone / Kate B Juergens / Eric Fujimura / Colin N O'Leary / Mamie Z Li / Joao A Paulo / Eric S Fischer / Siyuan ...Authors: Caleb R Glassman / Kheewoong Baek / Gaopeng Hou / Qiru Zeng / Christopher Nardone / Kate B Juergens / Eric Fujimura / Colin N O'Leary / Mamie Z Li / Joao A Paulo / Eric S Fischer / Siyuan Ding / J Wade Harper / Stephen J Elledge / ![]() Abstract: Viruses are intracellular parasites that reprogram the host proteome to promote replication and evade immune recognition. We applied a virome-wide library of ~10,000 open reading frames to discover ...Viruses are intracellular parasites that reprogram the host proteome to promote replication and evade immune recognition. We applied a virome-wide library of ~10,000 open reading frames to discover viral ubiquitin ligases, mapping their mechanisms of degradation and host substrates using targeted CRISPR screens and proteomics. These viral effectors could be classified as canonical ligases that mimic host E3s, hijackers that redirect host E3s, and non-canonical ligases that rewire Cullin-RING ligase machinery. These diverse strategies of virus-mediated degradation converged on immune-related substrates, including JAK1 and CUL1, underscoring immune evasion as a major driver of viral ubiquitin ligase evolution. Our findings elucidate viral strategies for exploiting the ubiquitin-proteasome system with potential for therapeutic targeting. | |||||||||||||||||||||||||||||||||
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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 | 9q3e.cif.gz | 180.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q3e.ent.gz | 129.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9q3e.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q3/9q3e ftp://data.pdbj.org/pub/pdb/validation_reports/q3/9q3e | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72190MC 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
| #1: Protein | Mass: 57744.199 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rotavirus A / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: B3SRV2 | ||||
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| #2: Protein | Mass: 13147.781 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15370 | ||||
| #3: Protein | Mass: 12485.135 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15369 | ||||
| #4: Protein | Mass: 89334.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: N-terminal fraction of CUL3 used for local refinement based structure. Source: (gene. exp.) Homo sapiens (human) / Gene: CUL3, KIAA0617 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q13618 | ||||
| #5: Chemical | | Has ligand of interest | Y | Has protein modification | N | |
-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: RotavirusA NSP1-ELOB-ELOC-CUL3 / Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
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| Source (natural) | Organism: Rotavirus A / Strain: B3SRV2.0.1 |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| 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: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50.6 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 173093 / Symmetry type: POINT |
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About Yorodumi




Rotavirus A
Homo sapiens (human)
United States, 1items
Citation
PDBj












Trichoplusia ni (cabbage looper)

FIELD EMISSION GUN