30YY
C6 symmetrized reconstruction of the adhesion device of the phage OE33PA
Summary for 30YY
| Entry DOI | 10.2210/pdb30yy/pdb |
| EMDB information | 58158 |
| Descriptor | distal tail protein (1 entity in total) |
| Functional Keywords | distail tail protein, adhesion device, siphophage, viral protein |
| Biological source | Oenococcus phage phiOE33PA |
| Total number of polymer chains | 6 |
| Total formula weight | 430473.00 |
| Authors | |
| 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 Cited by 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: 42244550DOI: 10.64898/2026.05.20.726473 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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