Summary for 8CD1
| Entry DOI | 10.2210/pdb8cd1/pdb |
| EMDB information | 16566 |
| Descriptor | 50S ribosomal protein L32, 50S ribosomal protein L4, 50S ribosomal protein L5, ... (54 entities in total) |
| Functional Keywords | phikz, phage, hijacked, bacterial, pseudomonas, phikz014, ribosome, 5s rrna |
| Biological source | Pseudomonas aeruginosa PAO1 More |
| Total number of polymer chains | 53 |
| Total formula weight | 2203921.72 |
| Authors | Gerovac, M.,Vogel, J. (deposition date: 2023-01-29, release date: 2024-01-24, Last modification date: 2024-11-06) |
| Primary citation | Gerovac, M.,Chihara, K.,Wicke, L.,Bottcher, B.,Lavigne, R.,Vogel, J. Phage proteins target and co-opt host ribosomes immediately upon infection. Nat Microbiol, 9:787-800, 2024 Cited by PubMed Abstract: Bacteriophages must seize control of the host gene expression machinery to replicate. To bypass bacterial anti-phage defence systems, this host takeover occurs immediately upon infection. A general understanding of phage mechanisms for immediate targeting of host transcription and translation processes is lacking. Here we introduce an integrative high-throughput approach to uncover phage-encoded proteins that target the gene expression machinery of Pseudomonas aeruginosa immediately upon infection with the jumbo phage ΦKZ. By integrating biochemical, genetic and structural analyses, we identify an abundant and conserved phage factor ΦKZ014 that targets the large ribosomal subunit by binding the 5S ribosomal RNA, and rapidly promotes replication in several clinical isolates. ΦKZ014 is among the earliest ΦKZ proteins expressed after infection and remains bound to ribosomes during the entire translation cycle. Our study provides a strategy to decipher molecular components of phage-mediated host takeover and argues that phage genomes represent an untapped discovery space for proteins that modulate the host gene expression machinery. PubMed: 38443577DOI: 10.1038/s41564-024-01616-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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