30YX
adhesion device (C3 symmetrized reconstruction) of the phage OE33PA
This is a non-PDB format compatible entry.
Summary for 30YX
| Entry DOI | 10.2210/pdb30yx/pdb |
| EMDB information | 58157 |
| Descriptor | Major tail protein, Distal tail protein, tail-associated dlysin, ... (5 entities in total) |
| Functional Keywords | distal tail protein, tail-associated lysin, tape measure protein, major tail protein, structural protein, viral protein |
| Biological source | Oenococcus phage phiOE33PA More |
| Total number of polymer chains | 21 |
| Total formula weight | 709357.04 |
| 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
Download full validation report
