8EGT

Capsid structure of Staphylococcus phage Andhra

8EGT の概要

• エントリーDOI: 10.2210/pdb8egt/pdb
• 関連するPDBエントリー: 8EGR 8EGS
• EMDBエントリー: 28128 28129 28130
• 分子名称: gp19, capsid lining protein, Major capsid protein (2 entities in total)
• 機能のキーワード: phage capsid, hk97-like fold, virus
• 由来する生物種: Staphylococcus phage Andhra; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 213978.95

構造登録者

Hawkins, N.C.,Kizziah, J.L.,Dokland, T. (登録日: 2022-09-13, 公開日: 2022-12-14, 最終更新日: 2024-06-19)

主引用文献

Hawkins, N.C.,Kizziah, J.L.,Hatoum-Aslan, A.,Dokland, T.
Structure and host specificity of Staphylococcus epidermidis bacteriophage Andhra.
Sci Adv, 8:eade0459-eade0459, 2022

PubMed Abstract: is an opportunistic pathogen of the human skin, often associated with infections of implanted medical devices. Staphylococcal picoviruses are a group of strictly lytic, short-tailed bacteriophages with compact genomes that are attractive candidates for therapeutic use. Here, we report the structure of the complete virion of -infecting phage Andhra, determined using high-resolution cryo-electron microscopy, allowing atomic modeling of 11 capsid and tail proteins. The capsid is a = 4 icosahedron containing a unique stabilizing capsid lining protein. The tail includes 12 trimers of a unique receptor binding protein (RBP), a lytic protein that also serves to anchor the RBPs to the tail stem, and a hexameric tail knob that acts as a gatekeeper for DNA ejection. Using structure prediction with AlphaFold, we identified the two proteins that comprise the tail tip heterooctamer. Our findings elucidate critical features for virion assembly, host recognition, and penetration.

PubMed: 36449623
DOI: 10.1126/sciadv.ade0459

実験手法

ELECTRON MICROSCOPY (3.5 Å)