Crystallization and preliminary crystallographic analysis of a novel haemolytic lectin from the mushroom Laetiporus sulphureus.
The novel haemolytic lectin from the parasitic mushroom Laetiporus sulphureus (LSL) is a homotetramer (approximately 140 kDa) composed of subunits associated by non-covalent bonds. It exhibits haemagglutination and haemolytic activities, both of which are inhibited by N-acetyllactosamine. The structural similarity found between LSL and the bacterial pore-forming toxins mosquitocidal toxin (MTX2) from Bacillus sphaericus and alpha-toxin from Clostridium septicum points to a mechanism of biological action involving the formation of pores in the target membranes. LSL has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality hexagonal crystals have unit-cell parameters a = b = 101.8, c = 193.9 angstroms and belong to space group P6(3)22. A 2.7 angstroms native data set was collected with an Rmerge of 9.2%.
Mancheño
José M
JM
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain. xjosemi@iqfr.csic.es
Tateno
Hiroaki
H
Goldstein
Irwin J
IJ
Hermoso
Juan A
JA
D000606:Amino Sugars / Q000737:chemistry; D001487:Basidiomycota / Q000201:enzymology*; D003013:Clostridium / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D019281:Dimerization; D004546:Elapid Venoms / Q000737:chemistry; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D009498:Neurotoxins / Q000737:chemistry; D011956:Receptors, Cell Surface / Q000378:metabolism; D030162:Reptilian Proteins; D013696:Temperature; D010738:Type C Phospholipases / Q000737:chemistry; D014961:X-Ray Diffraction
D000606:Amino Sugars; C405322:Bacillus sphaericus binary toxin receptor; D004546:Elapid Venoms; D037102:Lectins; D009498:Neurotoxins; D011956:Receptors, Cell Surface; D030162:Reptilian Proteins; C070124:muscarinic toxin 2; C000458:N-acetyllactosamine; D010738:Type C Phospholipases