Structural highlights
FunctionPublication Abstract from PubMedPhotorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity towards insect larvae. A hypothetical protein from P. luminescens was identified, purified from the native source and characterized as an L-fucose-binding lectin, named PLL. Glycan array and biochemical characterization data revealed PLL to be specific towards L-fucose and the disaccharide glycan 3,6-O-Me2-Glcbeta1-4(2,3-O-Me2)Rhaalpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homo-tetramer with an inter-subunit disulphide bridge. The crystal structures of native (ntPLL) and recombinant PLL (rPLL) revealed a seven-bladed beta-propeller fold creating 7 putative fucose-binding sites per monomer. The crystal structure of the rPLL/L-fucose complex confirmed at least three sites being fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C-terminus of the lectin into one of these sites. PLL exhibited a binding ability to insect haemocytes and the cuticular surface of a nematode, Heterorhabditis bacteriophora. A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Hepta-Bladed beta-Propeller Tetrameric Structure.,Kumar A, Sykorova P, Demo G, Dobes P, Hyrsl P, Wimmerova M J Biol Chem. 2016 Oct 7. pii: jbc.M115.693473. PMID:27758853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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