9LW6
Top cap of bacteriophage Mycofy1 mature head (C5 symmetry)
This is a non-PDB format compatible entry.
Summary for 9LW6
| Entry DOI | 10.2210/pdb9lw6/pdb |
| EMDB information | 63432 |
| Descriptor | Phage capsid-like C-terminal domain-containing protein (1 entity in total) |
| Functional Keywords | mycobacterium, bacteriophage, prolate head, major capsid protein, virus, viral protein |
| Biological source | Mycolicibacterium phage Mycofy1 |
| Total number of polymer chains | 54 |
| Total formula weight | 3227972.15 |
| Authors | |
| Primary citation | Li, X.,Shao, Q.,Li, L.,Xie, L.,Ruan, Z.,Fang, Q. Cryo-EM Reveals Structural Diversity in Prolate-headed Mycobacteriophage Mycofy1. J.Mol.Biol., 437:169126-169126, 2025 Cited by PubMed Abstract: Mycobacteriophages show promise in treating antibiotic-resistant mycobacterial infections. Here, we isolated Mycofy1, a mycobacteriophage, using M. smegmatis as a host. Cryo-EM analysis revealed that Mycofy1 possesses a prolate head and a long non-contractile tail. We determined structures of its head, head-to-tail interface, terminator, and tail tube to resolutions of ∼3.5 Å. Unexpectedly, we identified two distinct types of prolate head structures, exhibiting a 36° relative rotation in the top cap region. Additionally, the head-to-tail interface demonstrated flexibility. Our structures provide high-resolution cryo-EM data of a mycobacteriophage with a prolate head, as well as detailed structural information of the head-to-tail interface and head-proximal tail region in this phage group. These findings advance our understanding of assembly mechanisms in tailed bacteriophages. PubMed: 40187685DOI: 10.1016/j.jmb.2025.169126 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.42 Å) |
Structure validation
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