8WIM
Crystal structure of Jingmen tick virus RNA-dependent RNA polymerase (D307 construct)
8WIM の概要
エントリーDOI | 10.2210/pdb8wim/pdb |
分子名称 | Jingmen tick virus NSP1, MAGNESIUM ION, GLYCEROL, ... (5 entities in total) |
機能のキーワード | rna virus, flavi-like viruses, jingmen tick virus, rna-dependent rna polymerase, transferase |
由来する生物種 | Jingmen tick virus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 71813.32 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 38296832DOI: 10.1093/nar/gkae042 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.84 Å) |
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