National Center for
5J76: Structure Of Lectin From Colocasia Esculenta(l.) Schott
Int. J. Biol. Macromol. (2016) 91 p.518-523
The Mannose-binding beta-Prism Colocasia esculenta lectin (beta-PCL) was purified from tubers using ion exchange chromatography. The purified beta-PCL appeared as a single band of approximately 12kDa on SDS-PAGE. beta-PCL crystallizes in trigonal space group P3121 and diffracted to a resolution of 2.1A. The structure was solved using Molecular replacement using Crocus vernus lectin (PDB: 3MEZ) as a model. From the final refined model to an R-factor of 16.5% and an Rfree of 20.4%, it has been observed that the biological unit consists of two beta-Prism domains augmented through C-terminals swap over to form one of faces for each domain. Calpha superposition of individual domains of beta-PCL with individual domains of other related structures and superposition of whole protein structures were carried out. The higher RMS deviation for the superposition of whole structures suggest that beta-prism domains assume different orientation in each structure.