9B42
Pseudomonas phage Pa193 neck and extended tail (collar, gateway, tail tube, and sheath proteins)
Summary for 9B42
| Entry DOI | 10.2210/pdb9b42/pdb |
| EMDB information | 44166 |
| Descriptor | gp32 Sheath, gp29 Collar, gp33 Tail tube, ... (4 entities in total) |
| Functional Keywords | phage, bacteriophage, gene product (gp29), structural protein, viral protein, gene product 30 (gp30), collar protein, gateway protein, sheath protein, tail tube protein, gene product 32 (gp32), gene product 33 (gp33) |
| Biological source | Pseudomonas virus Pa193 More |
| Total number of polymer chains | 19 |
| Total formula weight | 368450.54 |
| 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 (3.5 Å) |
Structure validation
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