6OL3
Crystal structure of an adenovirus virus-associated RNA
Summary for 6OL3
Entry DOI | 10.2210/pdb6ol3/pdb |
Descriptor | Adenovirus Virus-Associated (VA) RNA I apical and central domains, POTASSIUM ION (3 entities in total) |
Functional Keywords | noncoding rna, viral rna, rna |
Biological source | Human adenovirus 2 |
Total number of polymer chains | 1 |
Total formula weight | 36161.57 |
Authors | Hood, I.V.,Gordon, J.M.,Bou-Nader, C.,Henderson, F.V.,Bahmanjah, S.,Zhang, J. (deposition date: 2019-04-15, release date: 2019-07-03, Last modification date: 2024-03-13) |
Primary citation | Hood, I.V.,Gordon, J.M.,Bou-Nader, C.,Henderson, F.E.,Bahmanjah, S.,Zhang, J. Crystal structure of an adenovirus virus-associated RNA. Nat Commun, 10:2871-2871, 2019 Cited by PubMed Abstract: Adenovirus Virus-Associated (VA) RNAs are the first discovered viral noncoding RNAs. By mimicking double-stranded RNAs (dsRNAs), the exceptionally abundant, multifunctional VA RNAs sabotage host machineries that sense, transport, process, or edit dsRNAs. How VA-I suppresses PKR activation despite its strong dsRNA character, and inhibits the crucial antiviral kinase to promote viral translation, remains largely unknown. Here, we report a 2.7 Å crystal structure of VA-I RNA. The acutely bent VA-I features an unusually structured apical loop, a wobble-enriched, coaxially stacked apical and tetra-stems necessary and sufficient for PKR inhibition, and a central domain pseudoknot that resembles codon-anticodon interactions and prevents PKR activation by VA-I. These global and local structural features collectively define VA-I as an archetypal PKR inhibitor made of RNA. The study provides molecular insights into how viruses circumnavigate cellular rules of self vs non-self RNAs to not only escape, but further compromise host innate immunity. PubMed: 31253805DOI: 10.1038/s41467-019-10752-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
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