Fig. 3: AtSLAC1 S59A structure is in a nonconductive, inactivated state.
a Pore depiction of the AtSLAC1 S59A structure. The anion conduction pore, calculated by HOLE240, is shown as red mesh. The structure is shown in a cartoon model, with the transmembrane domain colored slate blue, the N-terminus colored cyan, and the C-terminus colored yellow, respectively. The upper half of the channel is open to the periplasmic side of the cell, whereas the lower half is completely sealed. b Three ring-shaped layers of hydrophobic residues located along the anion path are shown in sticks. Each layer contains a phenylalanine residue, F276, F450 and F266. c Normalized inward current densities measured at −100 mV for the phenylalanine residue mutants compared to the WT AtSLAC1 characterized in the HEK293T cells. Independent experiments were repeated for each construct (WT, n = 10; F266A, n = 5; F276A, n = 5; F450A, n = 7; S59A, n = 6; S59A/F450A, n = 7). Significances were determined using one-way ANOVA with Dunnett’s multiple comparisons test for the single phenylalanine mutants, and unpaired t-test between the S59A and S59A/F450A mutants. *P = 0.0354 for the F276A mutant; **P = 0.0296 for the S59A/F450A mutant; **P = 0.0023 for the F266A mutant. Data are represented as mean ± S.E.M.
