9B41

Pseudomonas phage Pa193 Neck (portal and head-to-tail proteins)

Summary for 9B41

• Entry DOI: 10.2210/pdb9b41/pdb
• EMDB information: 44164
• Descriptor: gp19 Portal, gp28 Head-to-tail protein (2 entities in total)
• Functional Keywords: phage, bacteriophage, gene product (gp19), structural protein, viral protein, gene product 28 (gp28), head-to-tail protein, portal protein
• Biological source: Pseudomonas virus Pa193; More
• Total number of polymer chains: 24
• Total formula weight: 1216365.42

Authors

Iglesias, S.M.,Cingolani, G. (deposition date: 2024-03-20, release date: 2024-10-16)

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

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: 39370451
DOI: 10.1038/s42003-024-06985-x

Experimental method

ELECTRON MICROSCOPY (3.2 Å)