4RU5

Crystal Structure of the Pseudomonas phage phi297 tailspike gp61

4RU5 の概要

• エントリーDOI: 10.2210/pdb4ru5/pdb
• 分子名称: tailspike gp27, CALCIUM ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: beta-helix, tailspike, lyase
• 由来する生物種: Pseudomonas phage phi297
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 194513.52

構造登録者

Browning, C.,Sycheva, L.V.,Shneider, M.M.,Leiman, P.G. (登録日: 2014-11-18, 公開日: 2015-11-18, 最終更新日: 2024-02-28)

主引用文献

Olszak, T.,Shneider, M.M.,Latka, A.,Maciejewska, B.,Browning, C.,Sycheva, L.V.,Cornelissen, A.,Danis-Wlodarczyk, K.,Senchenkova, S.N.,Shashkov, A.S.,Gula, G.,Arabski, M.,Wasik, S.,Miroshnikov, K.A.,Lavigne, R.,Leiman, P.G.,Knirel, Y.A.,Drulis-Kawa, Z.
The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence.
Sci Rep, 7:16302-16302, 2017

PubMed Abstract: Pseudomonas phage LKA1 of the subfamily Autographivirinae encodes a tailspike protein (LKA1gp49) which binds and cleaves B-band LPS (O-specific antigen, OSA) of Pseudomonas aeruginosa PAO1. The crystal structure of LKA1gp49 catalytic domain consists of a beta-helix, an insertion domain and a C-terminal discoidin-like domain. The putative substrate binding and processing site is located on the face of the beta-helix whereas the C-terminal domain is likely involved in carbohydrates binding. NMR spectroscopy and mass spectrometry analyses of degraded LPS (OSA) fragments show an O5 serotype-specific polysaccharide lyase specificity. LKA1gp49 reduces virulence in an in vivo Galleria mellonella infection model and sensitizes P. aeruginosa to serum complement activity. This enzyme causes biofilm degradation and does not affect the activity of ciprofloxacin and gentamicin. This is the first comprehensive report on LPS-degrading lyase derived from a Pseudomonas phage. Biological properties reveal a potential towards its applications in antimicrobial design and as a microbiological or biotechnological tool.

PubMed: 29176754
DOI: 10.1038/s41598-017-16411-4

実験手法

X-RAY DIFFRACTION (1.52 Å)