9LW7

Midsection of bacteriophage Mycofy1 mature head (C5 symmetry)

Summary for 9LW7

• Entry DOI: 10.2210/pdb9lw7/pdb
• EMDB information: 63433
• 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: 12
• Total formula weight: 717327.14

Authors

Li, X.,Shao, Q.,Li, L.,Xie, L.,Ruan, Z.,Fang, Q. (deposition date: 2025-02-13, release date: 2025-04-16, Last modification date: 2025-04-30)

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

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: 40187685
DOI: 10.1016/j.jmb.2025.169126

Experimental method

ELECTRON MICROSCOPY (3.52 Å)