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PDBsum entry 4ru4
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Structural protein
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PDB id
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4ru4
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PDB id:
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| Name: |
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Structural protein
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Title:
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Crystal structure of the tailspike protein gp49 from pseudomonas phage lka1
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Structure:
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Tail spike protein gp49. Chain: a, b, c, d, e, f. Synonym: putative tail fiber protein. Engineered: yes
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Source:
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Pseudomonas phage lka1. Organism_taxid: 386793. Gene: gp49, pplka1_gp49. Expressed in: escherichia coli. Expression_system_taxid: 562. Site after his-tag)
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Resolution:
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1.90Å
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R-factor:
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0.132
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R-free:
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0.174
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Authors:
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C.Browning,M.M.Shneider,P.G.Leiman
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Key ref:
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T.Olszak
et al.
(2017).
The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence.
Sci Rep,
7,
16302.
PubMed id:
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Date:
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18-Nov-14
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Release date:
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18-Nov-15
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PROCHECK
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Headers
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References
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Q0E5W5
(Q0E5W5_9CAUD) -
Putative tail fiber protein from Pseudomonas phage LKA1
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Seq:
Struc:
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769 a.a.
589 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Sci Rep
7:16302
(2017)
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PubMed id:
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The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence.
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T.Olszak,
M.M.Shneider,
A.Latka,
B.Maciejewska,
C.Browning,
L.V.Sycheva,
A.Cornelissen,
K.Danis-Wlodarczyk,
S.N.Senchenkova,
A.S.Shashkov,
G.Gula,
M.Arabski,
S.Wasik,
K.A.Miroshnikov,
R.Lavigne,
P.G.Leiman,
Y.A.Knirel,
Z.Drulis-Kawa.
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ABSTRACT
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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.
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Links
