9JKC

Crystal structure of Aspergillus fumigatus polymycovirus 1 ploymerase (residues 85-763) in its apo state

9JKC の概要

• エントリーDOI: 10.2210/pdb9jkc/pdb
• 分子名称: RNA dependent RNA polymerase (2 entities in total)
• 機能のキーワード: rna virus, rna-dependent rna polymerase, viral protein
• 由来する生物種: Aspergillus fumigatus tetramycovirus 1
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 384566.17

構造登録者

Jia, H.,Cao, S.,Gong, P. (登録日: 2024-09-15, 公開日: 2025-03-26, 最終更新日: 2025-04-30)

主引用文献

Jia, H.,Liu, S.,Rao, G.,Liu, Q.,Wu, J.,Cao, S.,Gong, P.
An evolutionarily unique viral RdRP suggests a common dual-function feature of the priming element.
Sci Adv, 11:eadv9640-eadv9640, 2025

PubMed Abstract: Many RNA-dependent RNA polymerases (RdRPs) encoded by RNA viruses use de novo initiation strategy to start RNA synthesis, and they usually contain a priming element (PE) to interact with template RNA and priming nucleoside triphosphate to facilitate initiation. Upon transition to elongation in dengue virus 2 (DENV2) RdRP, PE refolds and contributes to elongation complex stability by interacting with the upstream RNA duplex. However, whether this PE dual-function feature commonly exists in viral RdRPs remains elusive, as PE is highly diverse among the entire RNA virus group. Here, a more complexed PE refolding is observed in RdRP crystal structures of polymycovirus-1 (AfuPmV-1), a polymycovirus evolutionarily connecting positive-strand and double-stranded RNA viruses. Although structural details and enzymology features are very different in transition from initiation to elongation in DENV2 and AfuPmV-1 RdRPs, what is in common is the PE dual-function feature that demonstrates functional conservation beyond sequence and structure.

PubMed: 40249801
DOI: 10.1126/sciadv.adv9640

実験手法

X-RAY DIFFRACTION (3.4 Å)