4ru5

<StructureSection load='4ru5' size='340' side='right' caption='[[4ru5]], [[Resolution|resolution]] 1.52&Aring;' scene=''>

<table><tr><td colspan='2'>[[4ru5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_bacteriophage_phi297 Pseudomonas aeruginosa bacteriophage phi297]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RU5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phi297_00061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1129145 Pseudomonas aeruginosa bacteriophage phi297])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ru5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ru5 OCA], [http://pdbe.org/4ru5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ru5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ru5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ru5 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

 

== References ==

[[Category: Pseudomonas aeruginosa bacteriophage phi297]]

[[Category: Browning, C]]

[[Category: Leiman, P G]]

[[Category: Shneider, M M]]

[[Category: Sycheva, L V]]

[[Category: Tailspike]]