Fig. 3: Mapping the binding sites of the specific inhibitors CATR and BKA.

a CPM thermostability data of each protein in absence of effectors (top), or in presence of CATR (middle) or BKA (bottom). The bars and error bars represent the mean and sample standard deviation of eight independent experiments for the wild type and 2–7 for the variants. Significance analysis for each condition was performed with one-way ANOVA, as described in “Methods”. Only the significant are indicated (p > 0.01, ns; p ≤ 0.01, *; p ≤ 0.001, **; p ≤ 0.0001, ***; p ≤ 0.00001, ****). b Lateral view of ScAac2 cytoplasmic-open state structure in complex with CATR (PDB code: 4c9h chain A). The interacting residues of ScAac2 are conserved in TtAac, with the exception of K104 which is R100 in TtAac and the two proteins share 74% sequence identity. To facilitate comparison, we used the TtAac labelling (Supplementary Fig. 3). Residues that form ionic interactions (yellow dashes) and hydrophobic contacts with CATR (marine) are shown in dark blue and brown, respectively. Residue K104 of ScAac2 has been modelled to Arg (R100) for TtAac. c Matrix view of the matrix-open structure of TtAac with BKA bound (PDB code: 6gci chain A). Residues that form ionic interactions (yellow dashes) or hydrogen bonds (black dashes) with BKA (orange) are shown in purple, while residues that form hydrophobic contacts are shown in cyan. Source data for this figure are provided as a Source Data file.