5j76

Publication Abstract from PubMed

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.

Structural analysis of beta-prism lectin from Colocasia esculenta (L.) S chott.,Vajravijayan S, Pletnev S, Pletnev VZ, Nandhagopal N, Gunasekaran K Int J Biol Macromol. 2016 Jun 1;91:518-523. doi: 10.1016/j.ijbiomac.2016.05.048. PMID:27262515^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.