9JLF

Cryo-EM Structure of Bacteriophage FCWL1 head-to-tail interface

Summary for 9JLF

• Entry DOI: 10.2210/pdb9jlf/pdb
• EMDB information: 61588
• Descriptor: Terminator protein, Tail tube protein, Portal protein, ... (5 entities in total)
• Functional Keywords: t1-like phage, neck, tail, viral protein
• Biological source: Escherichia phage FCWL1; More
• Total number of polymer chains: 8
• Total formula weight: 209050.32

Authors

Cai, C.,Wang, Y.,Liu, Y.,Shao, Q.,Wang, A.,Fang, Q. (deposition date: 2024-09-18, release date: 2025-01-22, Last modification date: 2025-07-02)

Primary citation

Cai, C.,Wang, Y.,Liu, Y.,Shao, Q.,Wang, A.,Li, L.,Zheng, Y.,Zhang, T.,Luo, Z.,Yang, C.,Fang, Q.
Structures of a T1-like siphophage reveal capsid stabilization mechanisms and high structural similarities with a myophage.
Structure, 33:663-676.e2, 2025

PubMed Abstract: Bacteriophage T1, a member of Siphoviruses, infects Escherichia coli with high efficiency, making it a promising candidate for phage therapy. Here, we report the near-atomic structures of FCWL1, a T1-like phage that belongs to the T1 phage family. We focus on the head, the head-to-tail interface, and its surrounding components. The hexameric capsomer displays unique gaps between neighboring A domains of the major capsid proteins. These gaps are partially filled by the N-loop of the decoration protein, which adopts a unique conformation. These structural features suggest that the phage might employ a novel strategy for stabilizing its head. Furthermore, despite being a siphophage, the head and head-to-tail connector of the phage show high structural similarity to those of a myophage. These findings enhance our understanding of the structure, capsid stabilization mechanism, and evolution of phages in the T1 family.

PubMed: 39914381
DOI: 10.1016/j.str.2025.01.012

Experimental method

ELECTRON MICROSCOPY (3.3 Å)