9WCB

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

This is a non-PDB format compatible entry.

Summary for 9WCB

• Entry DOI: 10.2210/pdb9wcb/pdb
• EMDB information: 65859
• Descriptor: A8 gpJ 713, Outer membrane porin C (2 entities in total)
• Functional Keywords: phage tail, viral protein
• Biological source: Escherichia phage Lambda; More
• Total number of polymer chains: 6
• Total formula weight: 257376.52

Authors

Deng, T.Y.,Ge, X.F.,Wang, J.W. (deposition date: 2025-08-16, release date: 2026-01-28, Last modification date: 2026-03-18)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.89 Å)