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-Structure paper
Title | Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation. |
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Journal, issue, pages | Nat Microbiol, Vol. 5, Issue 6, Page 864-871, Year 2020 |
Publish date | Apr 27, 2020 |
Authors | Panpan Wang / Lu Liu / Aijun Liu / Liming Yan / Yong He / Shu Shen / Mingxu Hu / Yu Guo / Haiguang Liu / Chuang Liu / Yinying Lu / Peiyi Wang / Fei Deng / Zihe Rao / Zhiyong Lou / |
PubMed Abstract | Segmented negative-sense RNA viruses (sNSRVs) encode a single-polypeptide polymerase (L protein) or a heterotrimeric polymerase complex to cannibalize host messenger RNA cap structures serving as ...Segmented negative-sense RNA viruses (sNSRVs) encode a single-polypeptide polymerase (L protein) or a heterotrimeric polymerase complex to cannibalize host messenger RNA cap structures serving as primers of transcription, and catalyse RNA synthesis. Here, we report the full-length structure of the severe fever with thrombocytopaenia syndrome virus (SFTSV) L protein, as determined by cryogenic electron microscopy at 3.4 Å, leading to an atomic model harbouring three functional parts (an endonuclease, an RNA-dependent RNA polymerase and a cap-binding domain) and two structural domains (an arm domain with a blocker motif and a carboxy-terminal lariat domain). The SFTSV L protein has a compact architecture in which its cap-binding pocket is surprisingly occupied by an Arg finger of the blocker motif, and the endonuclease active centre faces back towards the cap-binding pocket, suggesting that domain rearrangements are necessary to acquire the pre-initiation state of the active site. Our results provide insight into the complete architecture of sNSRV-encoded L protein and further the understanding of sNSRV transcription initiation. |
External links | Nat Microbiol / PubMed:32341479 |
Methods | EM (single particle) |
Resolution | 3.4 Å |
Structure data | |
Chemicals | ChemComp-MG: |
Source |
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Keywords | VIRAL PROTEIN / polymease / VIRUS |