9L01

Cryo-EM structure of bacteriophage T1 portal-adaptor

9L01 の概要

• エントリーDOI: 10.2210/pdb9l01/pdb
• EMDBエントリー: 62682
• 分子名称: adaptor protein, Putative portal protein (2 entities in total)
• 機能のキーワード: portal, adaptor, phage, viral protein
• 由来する生物種: Escherichia phage T1; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 762357.01

構造登録者

Chen, Y.,Liu, H.R. (登録日: 2024-12-11, 公開日: 2025-03-12, 最終更新日: 2025-09-24)

主引用文献

Chen, Y.,Xiao, H.,Zhou, J.,Peng, Z.,Peng, Y.,Song, J.,Zheng, J.,Liu, H.
The In Situ Structure of T-Series T1 Reveals a Conserved Lambda-Like Tail Tip.
Viruses, 17:-, 2025

PubMed Abstract: It is estimated that over 60% of known tailed phages are siphophages, which are characterized by a long, flexible, and non-contractile tail. Nevertheless, entire high-resolution structures of siphophages remain scarce. Using cryo-EM, we resolved the structures of T-series siphophage T1, encompassing its head, connector complex, tail tube, and tail tip, at near-atomic resolution. The density maps enabled us to build the atomic models for the majority of T1 proteins. The T1 head comprises 415 copies of the major capsid protein gp47, arranged into an icosahedron with a triangulation number of seven, decorated with 80 homologous trimers and 60 heterotrimers along the threefold and quasi-threefold axes of the icosahedron. The T1 connector complex is composed of two dodecamers (a portal and an adaptor) and two hexamers (a stopper and a tail terminator). The flexible tail tube comprises approximately 34 hexameric rings of tail tube. The extensive disulfide bond network along the successive tail rings may mediate the flexible bending. The distal tip of T1, which is cone-shaped and assembled by proteins gp33, gp34, gp36, gp37, and gp38, displays structural similarity to that of phage lambda. In conjunction with previous studies of lambda-like siphophages, our structure will facilitate further exploration of the structural and mechanistic aspects of lambda-like siphophages.

PubMed: 40143278
DOI: 10.3390/v17030351

実験手法

ELECTRON MICROSCOPY (3.6 Å)