8BFK

Jumbo Phage phi-kp24 tail inner tube

Summary for 8BFK

• Entry DOI: 10.2210/pdb8bfk/pdb
• EMDB information: 13862 14356 14357 15669 15669
• Descriptor: Putative virion structural protein (1 entity in total)
• Functional Keywords: jumbo phage, klebsiella pneumoniae, tail, sheath, structural protein
• Biological source: Klebsiella phage vB_KpM_FBKp24
• Total number of polymer chains: 18
• Total formula weight: 573387.37

Authors

Ouyang, R.,Briegel, A. (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

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: 36433970
DOI: 10.1038/s41467-022-34972-5

Experimental method

ELECTRON MICROSCOPY (3 Å)