| Autor: |
Latimer-Smith, Merlyn, Salgado, Paula S., Forsyth, Ismay, Makeyev, Eugene, Poranen, Minna M., Stuart, Dave I., Grimes, Jonathan M., El Omari, Kamel |
| Předmět: |
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| Zdroj: |
Scientific Reports; 10/12/2024, Vol. 14 Issue 1, p1-11, 11p |
| Abstrakt: |
The replication of RNA viruses relies on the activity of RNA-dependent RNA polymerases (RdRps). Despite large variations in their genomic sequences, viral RdRps share a common architecture generally known as a closed right hand. The P2 polymerase of cystovirus φ6 is currently among the best characterized viral RdRps. This polymerase is responsible for carrying out both replication and transcription of the viral double-stranded RNA genome using de novo initiation. Despite the extensive biochemical and structural studies conducted on φ6 P2, further structural information on other cystoviral RdRps is crucial to elucidate the structural and functional diversity of viral RdRps. Here, we have determined the atomic X-ray structure of the RdRp P2 from the φ6-related cystovirus φ8 at 3Å resolution. This structure completes the existing set of structural information on the φ8 polymerase complex and sheds light on the difference and similarities with related cystoviral RdRps. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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