8K35 の概要
| エントリーDOI | 10.2210/pdb8k35/pdb |
| EMDBエントリー | 36844 |
| 分子名称 | Tip attachment protein J, Tail tip protein L, Tail tip protein M, ... (7 entities in total) |
| 機能のキーワード | complex, viral protein |
| 由来する生物種 | Escherichia phage Lambda (Bacteriophage lambda) 詳細 |
| タンパク質・核酸の鎖数 | 24 |
| 化学式量合計 | 1028793.50 |
| 構造登録者 | |
| 主引用文献 | Xiao, H.,Tan, L.,Tan, Z.,Zhang, Y.,Chen, W.,Li, X.,Song, J.,Cheng, L.,Liu, H. Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly. Plos Biol., 21:e3002441-e3002441, 2023 Cited by PubMed Abstract: Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus-host cell interactions; moreover, it serves as a channel for genome delivery during infection. However, the in situ high-resolution structure of the neck-tail complex of siphophages remains unknown. Here, we present the structure of the siphophage lambda "wild type," the most widely used, laboratory-adapted fiberless mutant. The neck-tail complex comprises a channel formed by stacked 12-fold and hexameric rings and a 3-fold symmetrical tip. The interactions among DNA and a total of 246 tail protein molecules forming the tail and neck have been characterized. Structural comparisons of the tail tips, the most diversified region across the lambda and other long-tailed phages or tail-like machines, suggest that their tail tip contains conserved domains, which facilitate tail assembly, receptor binding, cell adsorption, and DNA retaining/releasing. These domains are distributed in different tail tip proteins in different phages or tail-like machines. The side tail fibers are not required for the phage particle to orient itself vertically to the surface of the host cell during attachment. PubMed: 38096144DOI: 10.1371/journal.pbio.3002441 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.44 Å) |
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