8BFL

Jumbo Phage phi-kp24 empty capsid hexamers

これはPDB形式変換不可エントリーです。

8BFL の概要

• エントリーDOI: 10.2210/pdb8bfl/pdb
• EMDBエントリー: 13862 14356 14357
• 分子名称: Major head protein (1 entity in total)
• 機能のキーワード: jumbo phage, klebsiella pheumoniae, capsid, virus
• 由来する生物種: Klebsiella phage vB_KpM_FBKp24
• タンパク質・核酸の鎖数: 42
• 化学式量合計: 2676829.64

構造登録者

Ouyang, R. (登録日: 2022-10-26, 公開日: 2022-12-07, 最終更新日: 2024-07-24)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4.1 Å)