30YU

Connector and Major Tail Protein of the phage OE33PA

これはPDB形式変換不可エントリーです。

30YU の概要

• エントリーDOI: 10.2210/pdb30yu/pdb
• EMDBエントリー: 58151
• 分子名称: portal protein, adaptor protein, stopper protein, ... (6 entities in total)
• 機能のキーワード: connector, major tail protein, siphophage, viral protein
• 由来する生物種: Oenococcus phage phiOE33PA; 詳細
• タンパク質・核酸の鎖数: 42
• 化学式量合計: 957449.98

構造登録者

Goulet, A.,Cambillau, C. (登録日: 2026-05-18, 公開日: 2026-06-17)

主引用文献

Schmitt, L.,Chaib, A.,Ptchelkine, D.,Kandiah, E.,Le Marrec, C.,Cambillau, C.,Goulet, A.
Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.
Biorxiv, 2026

PubMed Abstract: Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we report cryo-electron microscopy structures of the siphophage OE33PA, providing the first atomic resolution view of a phage infecting this bacterium important for the wine industry. While the overall virion architecture is conserved, the adhesion device displays distinctive features. Its receptor-binding proteins adopt multiple orientations, revealing an intrinsically dynamic assembly. cryo-electron tomography captures distinct conformations upon host attachment, providing rare structural insight into interactions with Gram-positive hosts. Additionally, functional assays show that a highly mobile carbohydrate-binding module in the distal tail protein mediates host-specific binding. Furthermore, the tape measure protein, central to phage assembly and infectivity, adopts a hexameric organization, updating the prevailing trimeric model in siphophages. Together, these findings reveal a dynamic adhesion device in a phage infecting Gram-positive bacteria and highlight the structural and functional diversity of phages.

PubMed: 42244550
DOI: 10.64898/2026.05.20.726473

実験手法

ELECTRON MICROSCOPY (3 Å)