A Novel Fucose-binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed β-Propeller Tetrameric Structure.

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-Me₂-Glcβ1-4(2,3-O-Me₂)Rhaα-O-(p-C₆H₄)-OCH₂CH₂NH₂ 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-bind

SUBMITTER: Kumar A 

PROVIDER: S-EPMC5122772 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature