- EMDB-45164: Structure of the Shigella flexneri bacteriophage Sf14 - tail helical -
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基本情報
登録情報
データベース: EMDB / ID: EMD-45164
タイトル
Structure of the Shigella flexneri bacteriophage Sf14 - tail helical
マップデータ
試料
ウイルス: Shigella phage Sf14 (ファージ)
タンパク質・ペプチド: Putative structural protein
タンパク質・ペプチド: gp40
キーワード
Sf14 / VIRUS
機能・相同性
Structural protein ORF10, bacteriophage KPP10 / Protein of unknown function DUF3383 / Bacteriophage KPP10, Structural protein ORF10 / Protein of unknown function (DUF3383) / Uncharacterized protein / Putative structural protein
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R01AI170608
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
U24GM116789
米国
引用
ジャーナル: Commun Biol / 年: 2025 タイトル: The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers. 著者: Sundharraman Subramanian / Hailey R Kerns / Samantha G Braverman / Sarah M Doore / 要旨: Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we ...Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we determined high-resolution structures of the Sf14 capsid and neck, along with a moderate-resolution structure of the whole Sf14 tail and baseplate. These structures indicate the capsid has not one, but two different types of decoration proteins: a trimeric β-tulip lattice that covers the entire capsid and a set of Hoc-like proteins that bind preferentially to hexamers at the quasi-3-fold axes of symmetry. The neck also contains two sets of whiskers oriented in opposite directions, and the tail has two types of long tail fibers which may bind different receptors. Based on homology and phylogenetic analysis, Sf14 may be the product of multiple horizontal gene transfer events. The structures presented here can be used to investigate further hypotheses of phage structure-function relationships and structural diversity.