8VJA
Cryo-EM of tail of bacteriophage Chi
8VJA の概要
エントリーDOI | 10.2210/pdb8vja/pdb |
EMDBエントリー | 43278 |
分子名称 | Tail Tube (1 entity in total) |
機能のキーワード | flagellotropic bacteriophage, siphophage, tail, virus |
由来する生物種 | Chivirus chi |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 40375.36 |
構造登録者 | |
主引用文献 | Sonani, R.R.,Esteves, N.C.,Scharf, B.E.,Egelman, E.H. Cryo-EM structure of flagellotropic bacteriophage Chi. Structure, 32:856-865.e3, 2024 Cited by PubMed Abstract: The flagellotropic bacteriophage χ (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil χ's nearly complete structure, encompassing capsid, neck, tail, and tail tip. While the capsid and tail resemble phage YSD1, the neck and tail tip reveal new proteins and their arrangement. The neck shows a unique conformation of the tail tube protein, forming a socket-like structure for attachment to the neck. The tail tip comprises four proteins, including distal tail protein (DTP), two baseplate hub proteins (BH1P and BH2P), and tail tip assembly protein (TAP) exhibiting minimal organization compared to other siphophages. Deviating from the consensus in other siphophages, DTP in χ forms a trimeric assembly, reducing tail symmetry from 6-fold to 3-fold at the tip. These findings illuminate the previously unexplored structural organization of χ's neck and tail tip. PubMed: 38614087DOI: 10.1016/j.str.2024.03.011 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.7 Å) |
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