8Z9R
Cryo-EM structure of Thogoto virus polymerase in a replication elongation-reception conformation
8Z9R の概要
エントリーDOI | 10.2210/pdb8z9r/pdb |
EMDBエントリー | 39868 |
分子名称 | Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (6 entities in total) |
機能のキーワード | rna polymerase, transcription |
由来する生物種 | Thogoto virus (isolate SiAr 126) (Tho) 詳細 |
タンパク質・核酸の鎖数 | 11 |
化学式量合計 | 518213.23 |
構造登録者 | |
主引用文献 | Xue, L.,Chang, T.,Li, Z.,Wang, C.,Zhao, H.,Li, M.,Tang, P.,Wen, X.,Yu, M.,Wu, J.,Bao, X.,Wang, X.,Gong, P.,He, J.,Chen, X.,Xiong, X. Cryo-EM structures of Thogoto virus polymerase reveal unique RNA transcription and replication mechanisms among orthomyxoviruses. Nat Commun, 15:4620-4620, 2024 Cited by PubMed Abstract: Influenza viruses and thogotoviruses account for most recognized orthomyxoviruses. Thogotoviruses, exemplified by Thogoto virus (THOV), are capable of infecting humans using ticks as vectors. THOV transcribes mRNA without the extraneous 5' end sequences derived from cap-snatching in influenza virus mRNA. Here, we report cryo-EM structures to characterize THOV polymerase RNA synthesis initiation and elongation. The structures demonstrate that THOV RNA transcription and replication are able to start with short dinucleotide primers and that the polymerase cap-snatching machinery is likely non-functional. Triggered by RNA synthesis, asymmetric THOV polymerase dimers can form without the involvement of host factors. We confirm that, distinctive from influenza viruses, THOV-polymerase RNA synthesis is weakly dependent of the host factors ANP32A/B/E in human cells. This study demonstrates varied mechanisms in RNA synthesis and host factor utilization among orthomyxoviruses, providing insights into the mechanisms behind thogotoviruses' broad-infectivity range. PubMed: 38816392DOI: 10.1038/s41467-024-48848-3 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.58 Å) |
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