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9LWA

Bacteriophage Mycofy1 distal head-to-tail interface (C6 symmetry)

Summary for 9LWA
Entry DOI10.2210/pdb9lwa/pdb
EMDB information63436
DescriptorHead-to-tail stopper, Terminator protein gp11, Major tail protein (3 entities in total)
Functional Keywordsmycobacterium, bacteriophage, prolate head, head-to-tail interface, connector protein, terminator protein, tail tube protein, virus, viral protein
Biological sourceMycolicibacterium phage Mycofy1
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Total number of polymer chains3
Total formula weight58430.00
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 citationLi, 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: 40187685
DOI: 10.1016/j.jmb.2025.169126
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.83 Å)
Structure validation

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