Figure 1. Structural map for GlucY and tGlucY.

The two homologous domains of Gluc are indicated by the teal background in the interior of the ring; cysteine residues are colored in red and those conserved between the homologous domains are marked with asterisks (*). Hydrophobicity is plotted around the ring according to the Kyte & Doolittle scale with darker purple being more hydrophobic; the hydrophilic pocket hypothesized to be involved in substrate recruitment is at the bottom of the ring. Cystine predictions are marked with solid grey lines (DiANNA 1.1) and dashed yellow lines (DISULFIND). Though the two algorithms differ slightly in their predictions, both identified two disulfides within each homologous domain. The 4luc mutation points (L47S, L57P, M60I) are shown in outlined blue text and the Monsta mutation points (F89W, I90L, H95E, Y97W) in outlined green text. The mutant residues are listed above each point. The location in the full-length sequence chosen for truncation (E117) is marked by a caret (^).