9KMH
The Composite Cryo-EM Structure of the Portal Vertex of Bacteriophage FCWL1
This is a non-PDB format compatible entry.
Summary for 9KMH
| Entry DOI | 10.2210/pdb9kmh/pdb |
| EMDB information | 62433 |
| Descriptor | Major capsid protein, Decoration protein, Portal protein, ... (8 entities in total) |
| Functional Keywords | t1-like phage, capsid, icosahedrally averaged, viral protein |
| Biological source | Escherichia phage FCWL1 More |
| Total number of polymer chains | 107 |
| Total formula weight | 2810480.66 |
| Authors | |
| 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 Cited by 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: 39914381DOI: 10.1016/j.str.2025.01.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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