9B40
Pseudomonas phage Pa193 5-fold vertex (capsid, decorating, and scaffolding proteins)
This is a non-PDB format compatible entry.
Summary for 9B40
| Entry DOI | 10.2210/pdb9b40/pdb |
| EMDB information | 44163 |
| Descriptor | gp26 Major capsid, gp25 Decorating protein, gp24 Scaffolding protein (3 entities in total) |
| Functional Keywords | phage, bacteriophage, gene product 24 (gp24), structural protein, viral protein, gene product 25 (gp25), scaffolding protein, decorating protein, major capsid protein, gene product 26 (gp26) |
| Biological source | Pseudomonas virus Pa193 More |
| Total number of polymer chains | 19 |
| Total formula weight | 782292.49 |
| Authors | |
| Primary citation | Iglesias, S.M.,Hou, C.D.,Reid, J.,Schauer, E.,Geier, R.,Soriaga, A.,Sim, L.,Gao, L.,Whitelegge, J.,Kyme, P.,Birx, D.,Lemire, S.,Cingolani, G. Cryo-EM analysis of Pseudomonas phage Pa193 structural components. Commun Biol, 7:1275-1275, 2024 Cited by PubMed Abstract: The World Health Organization has designated Pseudomonas aeruginosa as a critical pathogen for the development of new antimicrobials. Bacterial viruses, or bacteriophages, have been used in various clinical settings, commonly called phage therapy, to address this growing public health crisis. Here, we describe a high-resolution structural atlas of a therapeutic, contractile-tailed Pseudomonas phage, Pa193. We used bioinformatics, proteomics, and cryogenic electron microscopy single particle analysis to identify, annotate, and build atomic models for 21 distinct structural polypeptide chains forming the icosahedral capsid, neck, contractile tail, and baseplate. We identified a putative scaffolding protein stabilizing the interior of the capsid 5-fold vertex. We also visualized a large portion of Pa193 ~ 500 Å long tail fibers and resolved the interface between the baseplate and tail fibers. The work presented here provides a framework to support a better understanding of phages as biomedicines for phage therapy and inform engineering opportunities. PubMed: 39370451DOI: 10.1038/s42003-024-06985-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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