9Q3E
Cryo-EM structure of RotavirusA NSP1-ELOB-ELOC-CUL3
Summary for 9Q3E
| Entry DOI | 10.2210/pdb9q3e/pdb |
| EMDB information | 72190 |
| Descriptor | Non-structural protein 1, Elongin-B, Elongin-C, ... (5 entities in total) |
| Functional Keywords | viral effector, e3 ligase, nsp1, cul3, viral protein |
| Biological source | Rotavirus A More |
| Total number of polymer chains | 4 |
| Total formula weight | 172907.97 |
| Authors | Baek, K.,Glassman, C.R.,Fischer, E.S. (deposition date: 2025-08-18, release date: 2026-07-08, Last modification date: 2026-07-22) |
| Primary citation | Glassman, C.R.,Baek, K.,Hou, G.,Zeng, Q.,Nardone, C.,Juergens, K.B.,Fujimura, E.,O'Leary, C.N.,Li, M.Z.,Paulo, J.A.,Fischer, E.S.,Ding, S.,Harper, J.W.,Elledge, S.J. Virome-wide ubiquitin ligase discovery reveals diverse mechanisms of immune evasion. Science, 2026 Cited by PubMed 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 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. PubMed: 42424437DOI: 10.1126/science.aec6299 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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