3RIQ

Siphovirus 9NA tailspike receptor binding domain

3RIQ の概要

• エントリーDOI: 10.2210/pdb3riq/pdb
• 分子名称: Tailspike protein, GLYCEROL (3 entities in total)
• 機能のキーワード: right handed beta-helix, tailspike, endorhamnosidase, lipopolysaccharide, viral protein
• 由来する生物種: Siphovirus 9NA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59498.31

構造登録者

Andres, D.,Roske, Y.,Doering, C.,Heinemann, U.,Seckler, R.,Barbirz, S. (登録日: 2011-04-14, 公開日: 2012-02-29, 最終更新日: 2023-09-13)

主引用文献

Andres, D.,Roske, Y.,Doering, C.,Heinemann, U.,Seckler, R.,Barbirz, S.
Tail morphology controls DNA release in two Salmonella phages with one lipopolysaccharide receptor recognition system.
Mol.Microbiol., 83:1244-1253, 2012

PubMed Abstract: Bacteriophages use specific tail proteins to recognize host cells. It is still not understood to molecular detail how the signal is transmitted over the tail to initiate infection. We have analysed in vitro DNA ejection in long-tailed siphovirus 9NA and short-tailed podovirus P22 upon incubation with Salmonella typhimurium lipopolysaccharide (LPS). We showed for the first time that LPS alone was sufficient to elicit DNA release from a siphovirus in vitro. Crystal structure analysis revealed that both phages use similar tailspike proteins for LPS recognition. Tailspike proteins hydrolyse LPS O antigen to position the phage on the cell surface. Thus we were able to compare in vitro DNA ejection processes from two phages with different morphologies with the same receptor under identical experimental conditions. Siphovirus 9NA ejected its DNA about 30 times faster than podovirus P22. DNA ejection is under control of the conformational opening of the particle and has a similar activation barrier in 9NA and P22. Our data suggest that tail morphology influences the efficiencies of particle opening given an identical initial receptor interaction event.

PubMed: 22364412
DOI: 10.1111/j.1365-2958.2012.08006.x

実験手法

X-RAY DIFFRACTION (1.5 Å)