FIGURE 4.

Binding surfaces of the GDAP1 G-Site are incompatible with GSH binding. A, Arrangement of glutathione interacting residues within GST Mu (PDBid 1U87). Hydrogen bonding interactions are indicated as black dashes and van der Walls interactions are yellow dashes. For each interacting residue, the corresponding residue from a structural alignment of GDAP1 with GST Mu is indicated within a box and the box colored by whether the change is conservative (white) or not conservative (red). Corresponding residues within α2 are not known as it is disordered in GDAP1. B, Superposition of GDAP1 with GST Mu glutathione binding pockets. For orientation, the position of the canonical GST active site residue (S34) is shown in red. GDAP1 residues 76–78 which occlude the glutathione binding pocket are shown in white. C, Omit map for residues 76–81 (F_o-F_c map contoured at 3.0σ) shown in mesh while GDAP1 residues 76–81 are shown in sticks, D, Primary sequence alignment of GDAP1 (mouse and human) and GST Mu in the region around helix α2. The observed secondary structure of GST Mu is indicated in yellow cartoon below for reference