Summary for 8BFL
| Entry DOI | 10.2210/pdb8bfl/pdb |
| EMDB information | 13862 14356 14357 |
| Descriptor | Major head protein (1 entity in total) |
| Functional Keywords | jumbo phage, klebsiella pheumoniae, capsid, virus |
| Biological source | Klebsiella phage vB_KpM_FBKp24 |
| Total number of polymer chains | 42 |
| Total formula weight | 2676829.64 |
| Authors | Ouyang, R. (deposition date: 2022-10-26, release date: 2022-12-07, Last modification date: 2024-07-24) |
| Primary citation | Ouyang, R.,Costa, A.R.,Cassidy, C.K.,Otwinowska, A.,Williams, V.C.J.,Latka, A.,Stansfeld, P.J.,Drulis-Kawa, Z.,Briers, Y.,Pelt, D.M.,Brouns, S.J.J.,Briegel, A. High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers. Nat Commun, 13:7241-7241, 2022 Cited by PubMed Abstract: The Klebsiella jumbo myophage ϕKp24 displays an unusually complex arrangement of tail fibers interacting with a host cell. In this study, we combine cryo-electron microscopy methods, protein structure prediction methods, molecular simulations, microbiological and machine learning approaches to explore the capsid, tail, and tail fibers of ϕKp24. We determine the structure of the capsid and tail at 4.1 Å and 3.0 Å resolution. We observe the tail fibers are branched and rearranged dramatically upon cell surface attachment. This complex configuration involves fourteen putative tail fibers with depolymerase activity that provide ϕKp24 with the ability to infect a broad panel of capsular polysaccharide (CPS) types of Klebsiella pneumoniae. Our study provides structural and functional insight into how ϕKp24 adapts to the variable surfaces of capsulated bacterial pathogens, which is useful for the development of phage therapy approaches against pan-drug resistant K. pneumoniae strains. PubMed: 36433970DOI: 10.1038/s41467-022-34972-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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