8RKA

Connector complex of empty bacteriophage JBD30 particle computed in C12 symmetry

8RKA の概要

• エントリーDOI: 10.2210/pdb8rka/pdb
• EMDBエントリー: 19266
• 分子名称: Portal protein, DUF1320 domain-containing protein (2 entities in total)
• 機能のキーワード: bacteriophage jbd30, virion, connector complex, portal, adaptor, empty particle, virus
• 由来する生物種: Pseudomonas phage JBD30; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72946.51

構造登録者

Valentova, L.,Fuzik, T.,Plevka, P. (登録日: 2023-12-23, 公開日: 2024-08-14, 最終更新日: 2025-07-02)

主引用文献

Valentova, L.,Fuzik, T.,Novacek, J.,Hlavenkova, Z.,Pospisil, J.,Plevka, P.
Structure and replication of Pseudomonas aeruginosa phage JBD30.
Embo J., 43:4384-4405, 2024

PubMed Abstract: Bacteriophages are the most abundant biological entities on Earth, but our understanding of many aspects of their lifecycles is still incomplete. Here, we have structurally analysed the infection cycle of the siphophage Casadabanvirus JBD30. Using its baseplate, JBD30 attaches to Pseudomonas aeruginosa via the bacterial type IV pilus, whose subsequent retraction brings the phage to the bacterial cell surface. Cryo-electron microscopy structures of the baseplate-pilus complex show that the tripod of baseplate receptor-binding proteins attaches to the outer bacterial membrane. The tripod and baseplate then open to release three copies of the tape-measure protein, an event that is followed by DNA ejection. JBD30 major capsid proteins assemble into procapsids, which expand by 7% in diameter upon filling with phage dsDNA. The DNA-filled heads are finally joined with 180-nm-long tails, which bend easily because flexible loops mediate contacts between the successive discs of major tail proteins. It is likely that the structural features and replication mechanisms described here are conserved among siphophages that utilize the type IV pili for initial cell attachment.

PubMed: 39143239
DOI: 10.1038/s44318-024-00195-1

実験手法

ELECTRON MICROSCOPY (3.12 Å)