6ZIG
Topological model of the p2 virion baseplate in activated conformation (closed Tal trimer)
Summary for 6ZIG
| Entry DOI | 10.2210/pdb6zig/pdb |
| EMDB information | 11225 |
| Descriptor | Receptor binding protein, Distal tail protein, Baseplate protein gp16 (3 entities in total) |
| Functional Keywords | lactococcal siphophage p2, baseplate, receptor-binding protein, distal tail protein, tail-associated lysin, viral protein |
| Biological source | Lactococcus phage p2 More |
| Total number of polymer chains | 33 |
| Total formula weight | 1058818.73 |
| Authors | Spinelli, S.,Cambillau, C.,Goulet, A. (deposition date: 2020-06-26, release date: 2020-08-26, Last modification date: 2024-05-01) |
| Primary citation | Spinelli, S.,Tremblay, D.,Moineau, S.,Cambillau, C.,Goulet, A. Structural Insights into Lactococcal Siphophage p2 Baseplate Activation Mechanism. Viruses, 12:-, 2020 Cited by PubMed Abstract: Virulent phages infecting , an industry-relevant bacterium, pose a significant risk to the quality of the fermented milk products. Phages of the Skunavirus genus are by far the most isolated lactococcal phages in the cheese environments and phage p2 is the model siphophage for this viral genus. The baseplate of phage p2, which is used to recognize its host, was previously shown to display two conformations by X-ray crystallography, a rested state and an activated state ready to bind to the host. The baseplate became only activated and opened in the presence of Ca. However, such an activated state was not previously observed in the virion. Here, using nanobodies binding to the baseplate, we report on the negative staining electron microscopy structure of the activated form of the baseplate directly observed in the p2 virion, that is compatible with the activated baseplate crystal structure. Analyses of this new structure also established the presence of a second distal tail (Dit) hexamer as a component of the baseplate, the topology of which differs largely from the first one. We also observed an uncoupling between the baseplate activation and the tail tip protein (Tal) opening, suggesting an infection mechanism more complex than previously expected. PubMed: 32796652DOI: 10.3390/v12080878 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (42.2 Å) |
Structure validation
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