6ZIG

Topological model of the p2 virion baseplate in activated conformation (closed Tal trimer)

6ZIG の概要

• エントリーDOI: 10.2210/pdb6zig/pdb
• EMDBエントリー: 11225
• 分子名称: Receptor binding protein, Distal tail protein, Baseplate protein gp16 (3 entities in total)
• 機能のキーワード: lactococcal siphophage p2, baseplate, receptor-binding protein, distal tail protein, tail-associated lysin, viral protein
• 由来する生物種: Lactococcus phage p2; 詳細
• タンパク質・核酸の鎖数: 33
• 化学式量合計: 1058818.73

構造登録者

Spinelli, S.,Cambillau, C.,Goulet, A. (登録日: 2020-06-26, 公開日: 2020-08-26, 最終更新日: 2024-05-01)

主引用文献

Spinelli, S.,Tremblay, D.,Moineau, S.,Cambillau, C.,Goulet, A.
Structural Insights into Lactococcal Siphophage p2 Baseplate Activation Mechanism.
Viruses, 12:-, 2020

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: 32796652
DOI: 10.3390/v12080878

実験手法

ELECTRON MICROSCOPY (42.2 Å)