30YS

Capsid of the Oenococcus oeni phage OE33PA

Summary for 30YS

• Entry DOI: 10.2210/pdb30ys/pdb
• EMDB information: 58149
• Descriptor: Major Capsid Protein (1 entity in total)
• Functional Keywords: major capsid protein, siphophage, structural protein, viral protein
• Biological source: Oenococcus phage phiOE33PA
• Total number of polymer chains: 7
• Total formula weight: 316515.91

Authors

Goulet, A.,Cambillau, C. (deposition date: 2026-05-18, release date: 2026-06-17)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.8 Å)