4RU4

Crystal structure of the tailspike protein gp49 from Pseudomonas phage LKA1

Summary for 4RU4

• Entry DOI: 10.2210/pdb4ru4/pdb
• Descriptor: tail spike protein gp49, 1,2-ETHANEDIOL, SODIUM ION, ... (5 entities in total)
• Functional Keywords: tail spike protein, baseplate, phage lka1, lyase, structural protein
• Biological source: Pseudomonas phage LKA1
• Total number of polymer chains: 6
• Total formula weight: 376069.69

Authors

Browning, C.,Shneider, M.M.,Leiman, P.G. (deposition date: 2014-11-18, release date: 2015-11-18, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.903 Å)