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| Title | The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17). |
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| Journal, issue, pages | Nucleic Acids Res, Vol. 53, Issue 8, Year 2025 |
| Publish date | Apr 22, 2025 |
Authors | Karoline Raulf / Timm O Koller / Bertrand Beckert / Alexander Lepak / Martino Morici / Mario Mardirossian / Marco Scocchi / Gert Bange / Daniel N Wilson / ![]() |
| PubMed Abstract | Proline-rich antimicrobial peptides (PrAMPs) are produced as part of the innate immune response of animals, insects, and plants. The well-characterized mammalian PrAMP bactenecin-5 (Bac5) has been ...Proline-rich antimicrobial peptides (PrAMPs) are produced as part of the innate immune response of animals, insects, and plants. The well-characterized mammalian PrAMP bactenecin-5 (Bac5) has been shown to help fight bacterial infection by binding to the bacterial ribosome and inhibiting protein synthesis. In the absence of Bac5-ribosome structures, the binding mode of Bac5 and exact mechanism of action has remained unclear. Here, we present a cryo-electron microscopy structure of Bac5 in complex with the 70S ribosome from the Gram-negative marine bacterium Vibrio natriegens. The structure shows that, despite sequence similarity to Bac7 and other type I PrAMPs, Bac5 displays a completely distinct mode of interaction with the ribosomal exit tunnel. Bac5 overlaps with the binding site of both A- and P-site transfer RNAs bound at the peptidyltransferase center, suggesting that this type I PrAMP can interfere with late stages of translation initiation as well as early stages of elongation. Collectively, our study presents a ribosome structure from V. natriegens, a fast-growing bacterium that has interesting biotechnological and synthetic biology applications, as well as providing additional insights into the diverse binding modes that type I PrAMPs can utilize to inhibit protein synthesis. |
External links | Nucleic Acids Res / PubMed:40331629 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.7 - 2.8 Å |
| Structure data | EMDB-51946, PDB-9h90: EMDB-51947, PDB-9h91: |
| Chemicals | ![]() ChemComp-SCM: ![]() ChemComp-HOH: ![]() ChemComp-ZN: |
| Source |
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Keywords | RIBOSOME / Vibrio natriegens / Bac5 / Bactenecin 5 / 50S / V. natriegens |
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vibrio natriegens (bacteria)
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