6L42

Structure of severe fever with thrombocytopenia syndrome virus L protein

Summary for 6L42

• Entry DOI: 10.2210/pdb6l42/pdb
• EMDB information: 0828
• Descriptor: RNA polymerase, MAGNESIUM ION (2 entities in total)
• Functional Keywords: polymease, virus, viral protein
• Biological source: Phlebovirus WCH/97/HN/China/2011
• Total number of polymer chains: 1
• Total formula weight: 238838.10

Authors

Wang, P.,Lou, Z. (deposition date: 2019-10-15, release date: 2020-05-13, Last modification date: 2025-07-02)

Primary citation

Wang, P.,Liu, L.,Liu, A.,Yan, L.,He, Y.,Shen, S.,Hu, M.,Guo, Y.,Liu, H.,Liu, C.,Lu, Y.,Wang, P.,Deng, F.,Rao, Z.,Lou, Z.
Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation.
Nat Microbiol, 5:864-871, 2020

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 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.

PubMed: 32341479
DOI: 10.1038/s41564-020-0712-2

Experimental method

ELECTRON MICROSCOPY (3.4 Å)