According to its primary structure, the PITG_06016 gene encodes for one of the 7 glucokinases present in Phytophthora infestans PiGlcK-1, the causal agent of late blight disease. Currently, there are no structural studies of any of its enzymes, hence the determination of the three-dimensional (3D) structure of PiGlcK-1 becomes a significant contribution to the deduction of its functions, its interaction with ligands, and possible regulatory mechanisms. In this work we present the first structural model obtained by in silico tools for PiGlcK-1. For the prediction of this model, different algorithms were used to find the best annealing, refinement, and qualitative evaluation of them. A structural comparison of the predicted model with other structures of crystallized glucokinases enzymes allowed us to identify both the regions of interaction with their classical substrates (glucose and ATP) and those involved in the binding of other substrates such as fructose and ADP. In addition, we propose a possible recognition region of PPi, an activator of kinase activity that includes the GXGE motif, conserved in enzymes of the ribokinase (RK) family which distinguishes this PiGlcK-1 from a classical glucokinase. Accordingly, these findings suggest PPi-binding motif as potential targets for the development of inhibitors of PiGlcK-1 activity.
Phythophtora infestans, Glucokinase, Modeling structural, Molecular docking, PPi-binding motif