8WIL

Crystal structure of Jingmen tick virus RNA-dependent RNA polymerase (D55 construct)

Summary for 8WIL

• Entry DOI: 10.2210/pdb8wil/pdb
• Descriptor: Jingmen tick virus NSP1, MAGNESIUM ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: rna virus, flavi-like viruses, jingmen tick virus, rna-dependent rna polymerase, transferase
• Biological source: Jingmen tick virus
• Total number of polymer chains: 1
• Total formula weight: 101120.04

Authors

Wang, X.,Jing, X.,Deng, F.,Gong, P. (deposition date: 2023-09-24, release date: 2024-01-17, Last modification date: 2024-04-24)

Primary citation

Wang, X.,Jing, X.,Shi, J.,Liu, Q.,Shen, S.,Cheung, P.P.,Wu, J.,Deng, F.,Gong, P.
A jingmenvirus RNA-dependent RNA polymerase structurally resembles the flavivirus counterpart but with different features at the initiation phase.
Nucleic Acids Res., 52:3278-3290, 2024

PubMed Abstract: Jingmenviruses are a category of emerging segmented viruses that have garnered global attention in recent years, and are close relatives of the flaviviruses in the Flaviviridae family. One of their genome segments encodes NSP1 homologous to flavivirus NS5. NSP1 comprises both the methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRP) modules playing essential roles in viral genome replication and capping. Here we solved a 1.8-Å resolution crystal structure of the NSP1 RdRP module from Jingmen tick virus (JMTV), the type species of jingmenviruses. The structure highly resembles flavivirus NS5 RdRP despite a sequence identity less than 30%. NSP1 RdRP enzymatic properties were dissected in a comparative setting with several representative Flaviviridae RdRPs included. Our data indicate that JMTV NSP1 produces characteristic 3-mer abortive products similar to the hepatitis C virus RdRP, and exhibits the highest preference of terminal initiation and shorter-primer usage. Unlike flavivirus NS5, JMTV RdRP may require the MTase for optimal transition from initiation to elongation, as an MTase-less NSP1 construct produced more 4-5-mer intermediate products than the full-length protein. Taken together, this work consolidates the evolutionary relationship between the jingmenvirus group and the Flaviviridae family, providing a basis to the further understanding of their viral replication/transcription process.

PubMed: 38296832
DOI: 10.1093/nar/gkae042

Experimental method

X-RAY DIFFRACTION (2.1 Å)