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| Title | Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 1695, Year 2025 |
| Publish date | Feb 16, 2025 |
Authors | Zhiwei Gu / Xiaofei Ge / Jiawei Wang / ![]() |
| PubMed Abstract | F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile ...F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB from Listeria monocytogenes. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies. |
External links | Nat Commun / PubMed:39956822 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.88 - 3.42 Å |
| Structure data | EMDB-61073, PDB-9j1j: EMDB-61074, PDB-9j1k: EMDB-61075, PDB-9j1l: |
| Chemicals | ![]() ChemComp-FE: |
| Source |
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Keywords | VIRUS LIKE PARTICLE / Bacteriocin / bacteriophage / Siphoviridae / F-type tailocin / phage tail-like bacteriocins / Listeria monocytogenes / monocin / cryo-EM |
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listeria monocytogenes (bacteria)
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