9WCB

Open state of A8 gpJ 713 central tail fiber with OmpC G17 from E. coli EDL933

これはPDB形式変換不可エントリーです。

9WCB の概要

• エントリーDOI: 10.2210/pdb9wcb/pdb
• EMDBエントリー: 65859
• 分子名称: A8 gpJ 713, Outer membrane porin C (2 entities in total)
• 機能のキーワード: phage tail, viral protein
• 由来する生物種: Escherichia phage Lambda; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 257376.52

構造登録者

Deng, T.Y.,Ge, X.F.,Wang, J.W. (登録日: 2025-08-16, 公開日: 2026-01-28, 最終更新日: 2026-03-18)

主引用文献

Deng, T.,Ge, X.,Wang, J.
Structures of lambda-like phage A8 tail tip bound to OmpC provide insight into receptor recognition.
Structure, 2026

PubMed Abstract: Bacteriophage infection begins with the specific recognition of bacterial surface receptors by tail tip proteins, a decisive event that determines host specificity and triggers genome delivery. However, the structural principles underlying this process remain poorly understood. Here, we determined high-resolution cryo-electron microscopy (cryo-EM) structures of the engineered λ-like bacteriophage A8 gpJ713 in the unbound form and bound to the outer membrane porin OmpC. Comparisons with our previously determined structures of wild-type λ gpJ alone and bound to LamB reveal conserved receptor binding-induced conformational transitions across λ-like siphoviruses, defining a general mechanistic framework for tail-tip recognition. Guided by this framework, we restored stable binding to the previously incompatible OmpC G40 variant and converted OmpF into a functional receptor through a minimal loop deletion. These proof-of-concept receptor reprogramming experiments demonstrate the predictive power of our structural model and illustrate how targeted receptor engineering can complement directed evolution in developing therapeutic phages.

PubMed: 41763202
DOI: 10.1016/j.str.2026.02.002

実験手法

ELECTRON MICROSCOPY (3.89 Å)