Summary for 9J1L
Entry DOI | 10.2210/pdb9j1l/pdb |
Related | 9J1J 9J1K |
EMDB information | 61075 |
Descriptor | Alpha-amylase, FtbP, FtbO, ... (5 entities in total) |
Functional Keywords | bacteriocin, bacteriophage, siphoviridae, f-type tailocin, phage tail-like bacteriocins, listeria monocytogenes, monocin, cryo-em, virus like particle |
Biological source | Listeria monocytogenes More |
Total number of polymer chains | 15 |
Total formula weight | 293421.56 |
Authors | Wang, J.W.,Gu, Z.W. (deposition date: 2024-08-05, release date: 2025-01-08, Last modification date: 2025-03-05) |
Primary citation | Gu, Z.,Ge, X.,Wang, J. Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes. Nat Commun, 16:1695-1695, 2025 Cited by 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 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. PubMed: 39956822DOI: 10.1038/s41467-025-57075-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.28 Å) |
Structure validation
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