5C9P

Crystal structure of recombinant PLL lectin complexed with L-fucose from Photorhabdus luminescens at 1.75 A resolution

Summary for 5C9P

• Entry DOI: 10.2210/pdb5c9p/pdb
• Related: 5C9L 5C9O
• Descriptor: PLL lectin, alpha-L-fucopyranose, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lectin, seven-bladed beta-propeller, fucose-specific, sugar binding protein
• Biological source: Photorhabdus luminescens
• Total number of polymer chains: 1
• Total formula weight: 43358.36

Authors

Kumar, A.,Sykorova, P.,Demo, G.,Dobes, P.,Hyrsl, P.,Wimmerova, M. (deposition date: 2015-06-28, release date: 2016-10-19, Last modification date: 2024-10-23)

Primary citation

Kumar, A.,Sykorova, P.,Demo, G.,Dobes, P.,Hyrsl, P.,Wimmerova, M.
A Novel Fucose-binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure.
J.Biol.Chem., 291:25032-25049, 2016

PubMed Abstract: Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity toward insect larvae. A hypothetical protein from P. luminescens was identified, purified from the native source, and characterized as an l-fucose-binding lectin, named P. luminescens lectin (PLL). Glycan array and biochemical characterization data revealed PLL to be specific toward l-fucose and the disaccharide glycan 3,6-O-Me-Glcβ1-4(2,3-O-Me)Rhaα-O-(p-CH)-OCHCHNH PLL was discovered to be a homotetramer with an intersubunit disulfide bridge. The crystal structures of native and recombinant PLL revealed a seven-bladed β-propeller fold creating seven putative fucose-binding sites per monomer. The crystal structure of the recombinant PLL·l-fucose complex confirmed that at least three sites were 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 an ability to bind to insect hemocytes and the cuticular surface of a nematode, H. bacteriophora.

PubMed: 27758853
DOI: 10.1074/jbc.M115.693473

Experimental method

X-RAY DIFFRACTION (1.75 Å)