8XCJ

Open State of central tail fiber of bacteriophage lambda upon binding to LamB (gpJ713-LamB complex)

8XCJ の概要

• エントリーDOI: 10.2210/pdb8xcj/pdb
• EMDBエントリー: 38242 38244 38245
• 分子名称: Maltoporin, Tip attachment protein J (2 entities in total)
• 機能のキーワード: bacteriophage, caudovirales, siphoviridae, phage lambda, host recognition, lamb, cryo-em, virus
• 由来する生物種: Shigella sonnei; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 280841.54

構造登録者

Ge, X.F.,Wang, J.W. (登録日: 2023-12-09, 公開日: 2024-05-01, 最終更新日: 2025-07-02)

主引用文献

Ge, X.,Wang, J.
Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor.
Nat Commun, 15:4185-4185, 2024

PubMed Abstract: Bacteriophage infection, a pivotal process in microbiology, initiates with the phage's tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. Although comprehensive studies on the interaction between bacteriophage lambda and its outer membrane receptor, LamB, have provided rich information about the system's biochemical properties, the precise molecular mechanism remains undetermined. This study revealed the high-resolution cryo-electron microscopy (cryo-EM) structures of the bacteriophage lambda tail complexed with its irreversible Shigella sonnei 3070 LamB receptor and the closed central tail fiber. These structures reveal the complex processes that trigger infection and demonstrate a substantial conformational change in the phage lambda tail tip upon LamB binding. Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in the fields of microbiology and therapeutic development.

PubMed: 38760367
DOI: 10.1038/s41467-024-48686-3

実験手法

ELECTRON MICROSCOPY (2.98 Å)