9Q2G

Phosphodiesterase from Burkholderia phage BCSR5 in the closed lid conformation

9Q2G の概要

• エントリーDOI: 10.2210/pdb9q2g/pdb
• 分子名称: Anti-CBASS protein Acb1, CITRATE ANION (3 entities in total)
• 機能のキーワード: phosphodiesterase, viral protein
• 由来する生物種: Burkholderia phage BCSR5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19164.69

構造登録者

Doherty, E.E.,Doudna, J.A. (登録日: 2025-08-15, 公開日: 2025-11-05, 最終更新日: 2026-01-28)

主引用文献

Doherty, E.E.,Nomburg, J.,Adler, B.A.,Lopez, S.,Hsieh, K.,Price, N.,Blount, N.,Doudna, J.A.
Divergent viral phosphodiesterases for immune signaling evasion.
Cell Host Microbe, 33:2043-2051.e6, 2025

PubMed Abstract: Cyclic dinucleotides (CDNs) and other short oligonucleotides play fundamental roles in immune system activation in organisms ranging from bacteria to humans. In response, viruses use phosphodiesterase (PDE)-mediated oligonucleotide cleavage for immune evasion, a strategy whose diversity has not yet been explored. Here, we use a canonical 2H PDE (2H PDE) structure-based search of prokaryotic and eukaryotic viral sequences to identify an exceptional diversity of 2H PDEs across the virome, including enzymes not detectable with sequence search methods alone. Despite active site conservation, biochemical experiments reveal remarkable substrate specificity of these PDEs that corresponds to variations in the core 2H fold. This nuanced specificity allows 2H PDEs to selectively degrade oligonucleotide messengers to avoid interfering with host nucleotide signaling. Together, these findings nominate viral 2H PDEs as key regulators of CDN signaling across the tree of life.

PubMed: 41297541
DOI: 10.1016/j.chom.2025.10.018

実験手法

X-RAY DIFFRACTION (2 Å)