Structure of the Trehalose-6-phosphate Phosphatase from Brugia malayi Reveals Key Design Principles for Anthelmintic Drugs
Figure 2
Structure of B. malayi T6PP and ortholog.
Ribbon diagram of the X-ray crystal structure of T6PP from Brugia malayi with selected helices or strands labeled (PDB ID 4OFZ) with the MIT-like domain (green), connector region (purple) the catalytic core Rossmann-fold HAD domain (blue) and the HAD cap domain (gold) colored differentially (A). A single magnesium ion (magenta sphere) marks the active site. The T. acidophilum T6PP-like enzyme lacks the MIT-like domain found in B. malayi (B). An overlay of these enzymes reveals a slightly more closed cap orientation in the T. acidophylum enzyme, but a nearly identical conformation of the C1 loop (rmsd = 1.04 Å mainchain atoms) (C and above). This molecular figure and all others, unless otherwise noted, were generated with UCSF Chimera v1.8.