8Y6V
Near-atomic structure of icosahedrally averaged jumbo bacteriophage PhiKZ capsid
This is a non-PDB format compatible entry.
Summary for 8Y6V
| Entry DOI | 10.2210/pdb8y6v/pdb |
| EMDB information | 39002 |
| Descriptor | gp28, gp184, gp244, ... (11 entities in total) |
| Functional Keywords | phikz, capsid protein, viral assembly, pseudomonas aeruginosa, jumbo phage, virus |
| Biological source | Phikzvirus phiKZ More |
| Total number of polymer chains | 42 |
| Total formula weight | 2785498.19 |
| Authors | |
| Primary citation | Yang, Y.,Shao, Q.,Guo, M.,Han, L.,Zhao, X.,Wang, A.,Li, X.,Wang, B.,Pan, J.A.,Chen, Z.,Fokine, A.,Sun, L.,Fang, Q. Capsid structure of bacteriophage Phi KZ provides insights into assembly and stabilization of jumbo phages. Nat Commun, 15:6551-6551, 2024 Cited by PubMed Abstract: Jumbo phages are a group of tailed bacteriophages with large genomes and capsids. As a prototype of jumbo phage, ΦKZ infects Pseudomonas aeruginosa, a multi-drug-resistant (MDR) opportunistic pathogen leading to acute or chronic infection in immunocompromised individuals. It holds potential to be used as an antimicrobial agent and as a model for uncovering basic phage biology. Although previous low-resolution structural studies have indicated that jumbo phages may have more complicated capsid structures than smaller phages such as HK97, the detailed structures and the assembly mechanism of their capsids remain largely unknown. Here, we report a 3.5-Å-resolution cryo-EM structure of the ΦKZ capsid. The structure unveiled ten minor capsid proteins, with some decorating the outer surface of the capsid and the others forming a complex network attached to the capsid's inner surface. This network seems to play roles in driving capsid assembly and capsid stabilization. Similar mechanisms of capsid assembly and stabilization are probably employed by many other jumbo viruses. PubMed: 39095371DOI: 10.1038/s41467-024-50811-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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