Fig. 2: A conserved negatively charged residue, Glu112, in the p20 domain contributes to AtMC9 activation and substrate processing.
From: Structural determinants for pH-dependent activation of a plant metacaspase
a Comparison of the interactions involving Glu112 at three different pHs. b Comparison of representative frames of the pH 4.2 (gray), 5.5 (purple), and 7.5 (green/marine/orange) simulations showing interactions involving Glu112. Interactions at each pH are displayed as each pH’s respective color but with pH 7.5 displayed as red. c Self-cleavage in E112K. For the wild-type (WT) sample, pH 8 was used in the incubation to compare with the mutant. Data are representative of two independent experiments. d Substrate GST-PROPEP1 processing by E112K. Data are representative of two independent experiments. Source data are provided as a Source Data file.
