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| Natura: | Artículo científico |
| Lingua: | en |
| Pubblicazione: |
Nucleic acids research
2025
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| Soggetti: | |
| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/40331629/ |
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| author | Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N |
| author_facet | Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N |
| collection | PubMed - marine biology |
| contents | The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17). Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N Vibrio Cryoelectron Microscopy Ribosomes Binding Sites Antimicrobial Peptides Models, Molecular Protein Biosynthesis Protein Binding Proline Peptides, Cyclic 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. |
| format | Artículo científico |
| id | pubmed_40331629 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Nucleic acids research |
| record_format | pubmed |
| spellingShingle | The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17). Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N Vibrio Cryoelectron Microscopy Ribosomes Binding Sites Antimicrobial Peptides Models, Molecular Protein Biosynthesis Protein Binding Proline Peptides, Cyclic The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17). Raulf, Karoline Koller, Timm O Beckert, Bertrand Lepak, Alexander Morici, Martino Mardirossian, Mario Scocchi, Marco Bange, Gert Wilson, Daniel N Vibrio Cryoelectron Microscopy Ribosomes Binding Sites Antimicrobial Peptides Models, Molecular Protein Biosynthesis Protein Binding Proline Peptides, Cyclic 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. |
| title | The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17). |
| topic | Vibrio Cryoelectron Microscopy Ribosomes Binding Sites Antimicrobial Peptides Models, Molecular Protein Biosynthesis Protein Binding Proline Peptides, Cyclic |
| url | https://pubmed.ncbi.nlm.nih.gov/40331629/ |