5C9L: Crystal structure of native PLL lectin from Photorhabdus luminescens at 1.65 A resolution

Citation:
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-Glcbeta1-4(2,3-O-Me2)Rhaalpha-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 beta-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.
PDB ID: 5C9LDownload
MMDB ID: 144070
PDB Deposition Date: 2015/6/27
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 1.65  Å
Source Organism:
Similar Structures:
Biological Unit for 5C9L: tetrameric; determined by author and by software (PISA)
Molecular Components in 5C9L
Label Count Molecule
Proteins (4 molecules)
4
PLL Lectin
Molecule annotation
Chemicals (59 molecules)
1
7
2
8
3
4
4
8
5
32
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.