Insilico structural modeling of normal and mutated subunits of ADP-glucose pyrophosphorylasefrom Triticum aestivum to study protein-protein interactions

Abstract

ADP-glucose pyrophosphorylase is a heterotetrameric enzyme with pairs of large subunits (LS) and small subunits (SS) involved in starch biosynthesis. The increase in grain yield and plant biomass is brought about by the deregulation of endosperm. Thus, AGPase has attracted widespread interest in improving starch content in crop improvement. The data herein conclusively shows that mutation insertion involved in conformational changes is responsible for the decrease in a pocket in the mutated subunit. This type of conformational change might be beneficial for better protein-protein interaction. The present study is aimed to model and compare the structure of normal and mutatedlarge subunits of wheat AGPase to studytheir structural differences. Mutations by insertion are involved in conformational changes that are responsible for the decrease in the pocket in the mutated subunit. Such conformational changes are often beneficial to study PPI (protein-protein interactions). Further investigations were carried out using docking studies to gain insight into interaction. Based on these studies, it may be suggested that such type of mutationsare usually beneficial for starch production in wheat which is considered one of the significant Indian food crops.