Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX110DE, UK.
Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
Sci Rep. 2024 Oct 9;14(1):23540. doi: 10.1038/s41598-024-75213-7.
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.
RNA 病毒的复制依赖于 RNA 依赖性 RNA 聚合酶（RdRps）的活性。尽管它们的基因组序列存在很大差异，但病毒 RdRps 具有共同的结构，通常被称为封闭的右手结构。囊状病毒 φ6 的 P2 聚合酶目前是研究最为深入的病毒 RdRps 之一。该聚合酶负责使用从头开始的方式进行病毒双链 RNA 基因组的复制和转录。尽管对 φ6 P2 进行了广泛的生化和结构研究，但获得其他囊状病毒 RdRps 的更多结构信息对于阐明病毒 RdRps 的结构和功能多样性至关重要。在这里，我们以 3Å 的分辨率确定了与 φ6 相关的囊状病毒 φ8 的 RdRp P2 的原子 X 射线结构。该结构完成了现有的 φ8 聚合酶复合物的结构信息集，并揭示了与相关囊状病毒 RdRps 的差异和相似之处。
