Crystallization and preliminary X-ray diffraction analysis of the seed lectin from Parkia platycephala.
The crystallization and preliminary X-ray diffraction analysis of the seed lectin of Parkia platycephala, a Mimosoideae, regarded as the most primitive group of the Leguminosae plants, are reported. Its amino-acid sequence consists of three tandemly arranged jacalin-related beta-prism domains, which is a novel fold for a leguminous lectin. Furthermore, no other lectin structure with this arrangement of domains has been described. P2(1)2(1)2(1) crystals (unit-cell parameters a = 63.6, b = 68.5, c = 208.5 A), which diffract to a maximum resolution of 2.2 A, were obtained in hanging drops at pH 8 and 293 K by the vapor-diffusion method using 10% 2-propanol and 20% polyethylene glycol 4000 as precipitants. The asymmetric unit contains two lectin molecules and has a solvent content of 46%. Only a single beta-prism domain could be located by molecular replacement using the structure of the Helianthus tuberosus lectin (PDB code 1c3k) as the search model. Isomorphous heavy-atom derivatives are currently being produced to solve the complete structure of the P. platycephala seed lectin.
Gallego del Sol
Francisca
F
Instituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, E-46010 Valencia, Spain.
Ramón-Maiques
Santiago
S
Santos
Claudia F
CF
Grangeiro
Thalles B
TB
Nagano
Celso S
CS
Farias
Creuza M S A
CM
Cavada
Benildo S
BS
Calvete
Juan J
JJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D007887:Fabaceae / Q000737:chemistry* / Q000196:embryology; D037102:Lectins / Q000737:chemistry*; D037121:Plant Lectins; D011487:Protein Conformation; D012639:Seeds / Q000737:chemistry*
D037102:Lectins; D037121:Plant Lectins