9H1Q

Structure of the borna disease virus 1 replication core complex - reaction complex

9H1Q の概要

• エントリーDOI: 10.2210/pdb9h1q/pdb
• EMDBエントリー: 51770
• 分子名称: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
• 機能のキーワード: polymerase, phosphoprotein, bornavirus, rdrp, viral protein
• 由来する生物種: Borna disease virus 1; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 295480.21

構造登録者

Keown, J.R.,Carrique, L.,Grimes, J.M. (登録日: 2024-10-10, 公開日: 2025-08-20, 最終更新日: 2026-03-04)

主引用文献

Carrique, L.,Gunl, F.,Deng, A.,Grimes, J.M.,Keown, J.R.
The structure of the mammalian bornavirus polymerase complex.
Nat Commun, 16:7508-7508, 2025

PubMed Abstract: Borna disease virus 1 (BoDV-1) is a non-segmented RNA virus with one of the smallest known RNA virus genomes. BoDV-1 replicates in the nucleus of infected cells using a virally encoded polymerase complex composed of the large protein and phosphoprotein. Here, we present the BoDV-1 polymerase complex at resolutions up to 2.8 Å, describing the fully ordered large polymerase protein bound to tetrameric phosphoprotein. The complex is maintained through the ordered C-terminal region of one copy of the phosphoprotein. Analysis of the model reveals a conserved methyltransferase domain, though key S-adenosyl methionine binding residues are missing. While no RNA is observed in our models, analysis of a sample under reaction conditions induces an opening and closing of the template entry and exit channels, respectively. Higher-order polymerase assemblies suggest oligomerisation as a conserved feature of negative strand RNA virus polymerases. We provide a molecular framework to investigate bornavirus replication and transcription.

PubMed: 40804239
DOI: 10.1038/s41467-025-62906-4

実験手法

ELECTRON MICROSCOPY (2.95 Å)