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9B45

Pseudomonas phage Pa193 baseplate complex and tail fiber

This is a non-PDB format compatible entry.
Summary for 9B45
Entry DOI10.2210/pdb9b45/pdb
EMDB information44168
Descriptorgp45-a Baseplate wedge 1, gp35 Sheath initiator, gp44 Tail tip, ... (11 entities in total)
Functional Keywordsphage, bacteriophage, baseplate complex, structural protein, viral protein, tail fiber
Biological sourcePseudomonas virus Pa193
More
Total number of polymer chains54
Total formula weight1989485.08
Authors
Iglesias, S.M.,Cingolani, G. (deposition date: 2024-03-20, release date: 2024-10-16)
Primary citationIglesias, 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: 39370451
DOI: 10.1038/s42003-024-06985-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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