Structure of the Trehalose-6-phosphate Phosphatase from Brugia malayi Reveals Key Design Principles for Anthelmintic Drugs
Figure 5
Proposed model of trehalose 6-phosphate in the active site of T6PP.
The FTMap server was used to identify hot spots where protein-substrate interactions may occur. Analysis of the T6PP enzyme from T. acidophilium (1U02) (A), and B. malayi (B) reveal hot spots near the interface of the cap and core domains. These hot spots are cradled by the structurally conserved C1-Loop. T6P was placed manually into the active site of T6PP by coordinating the Mg2+ cation with the phosphate group (C). The residues identified as important via mutagenesis and kinetics are labeled and can be seen in proximity to the trehalose moiety.