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Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
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...
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Published in: | Nature communications 2025-02, Vol.16 (1), p.1695, Article 1695 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | 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.
F-type phage-tail like bacteriocins (PTLBs) are protein complexes with bactericidal activity and share similarity with non-contractile phage tails. Here, authors report the atomic structure of monocin, an F-type PTLB from listeria monocytogenes. |
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ISSN: | 2041-1723 2041-1723 |
DOI: | 10.1038/s41467-025-57075-3 |