5NGJ

Crystal structure of pb6, major tail tube protein of bacteriophage T5

5NGJ の概要

• エントリーDOI: 10.2210/pdb5ngj/pdb
• 分子名称: Tail tube protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: bacteriophage, viral protein, tube protein, virion protein
• 由来する生物種: Escherichia phage T5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104457.23

構造登録者

Arnaud, C.-A.,Effantin, G.,Vives, C.,Engilberge, S.,Bacia, M.,Boulanger, P.,Girard, E.,Schoehn, G.,Breyton, C. (登録日: 2017-03-17, 公開日: 2018-01-03, 最終更新日: 2024-05-08)

主引用文献

Arnaud, C.A.,Effantin, G.,Vives, C.,Engilberge, S.,Bacia, M.,Boulanger, P.,Girard, E.,Schoehn, G.,Breyton, C.
Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection.
Nat Commun, 8:1953-1953, 2017

PubMed Abstract: The vast majority of phages, bacterial viruses, possess a tail ensuring host recognition, cell wall perforation and safe viral DNA transfer from the capsid to the host cytoplasm. Long flexible tails are formed from the tail tube protein (TTP) polymerised as hexameric rings around and stacked along the tape measure protein (TMP). Here, we report the crystal structure of T5 TTP pb6 at 2.2 Å resolution. Pb6 is unusual in forming a trimeric ring, although structure analysis reveals homology with all classical TTPs and related tube proteins of bacterial puncturing devices (type VI secretion system and R-pyocin). Structures of T5 tail tubes before and after interaction with the host receptor were determined by cryo-electron microscopy at 6 Å resolution. Comparison of these two structures reveals that host-binding information is not propagated to the capsid through conformational changes in the tail tube, suggesting a role of the TMP in this information transduction process.

PubMed: 29209037
DOI: 10.1038/s41467-017-02049-3

実験手法

X-RAY DIFFRACTION (2.2 Å)