8HQZ

Baseplate of DT57C bacteriophage in the full state

これはPDB形式変換不可エントリーです。

8HQZ の概要

• エントリーDOI: 10.2210/pdb8hqz/pdb
• EMDBエントリー: 34920 34949 34952 34955
• 分子名称: Baseplate hub protein, Distal tail protein, Minor tail protein, ... (7 entities in total)
• 機能のキーワード: baseplate, t5, virus, viral protein
• 由来する生物種: Escherichia phage DT57C; 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 773020.44

構造登録者

Ayala, R.,Moiseenko, A.V.,Chen, T.H.,Kulikov, E.E.,Golomidova, A.K.,Orekhov, P.S.,Street, M.A.,Sokolova, O.S.,Letarov, A.V.,Wolf, M. (登録日: 2022-12-14, 公開日: 2023-12-13, 最終更新日: 2025-06-18)

主引用文献

Ayala, R.,Moiseenko, A.V.,Chen, T.H.,Kulikov, E.E.,Golomidova, A.K.,Orekhov, P.S.,Street, M.A.,Sokolova, O.S.,Letarov, A.V.,Wolf, M.
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.
Nat Commun, 14:8205-8205, 2023

PubMed Abstract: The T5 family of viruses are tailed bacteriophages characterized by a long non-contractile tail. The bacteriophage DT57C is closely related to the paradigmal T5 phage, though it recognizes a different receptor (BtuB) and features highly divergent lateral tail fibers (LTF). Considerable portions of T5-like phages remain structurally uncharacterized. Here, we present the structure of DT57C determined by cryo-EM, and an atomic model of the virus, which was further explored using all-atom molecular dynamics simulations. The structure revealed a unique way of LTF attachment assisted by a dodecameric collar protein LtfC, and an unusual composition of the phage neck constructed of three protein rings. The tape measure protein (TMP) is organized within the tail tube in a three-stranded parallel α-helical coiled coil which makes direct contact with the genomic DNA. The presence of the C-terminal fragment of the TMP that remains within the tail tip suggests that the tail tip complex returns to its original state after DNA ejection. Our results provide a complete atomic structure of a T5-like phage, provide insights into the process of DNA ejection as well as a structural basis for the design of engineered phages and future mechanistic studies.

PubMed: 38081816
DOI: 10.1038/s41467-023-43824-9

実験手法

ELECTRON MICROSCOPY (3.8 Å)