Fig. 1: Structures of Arabidopsis thaliana SLAC1 6D mutant in open and closed conformations. | Nature Communications

Fig. 1: Structures of Arabidopsis thaliana SLAC1 6D mutant in open and closed conformations.

From: Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model

Fig. 1

a I-V relationship of AtSLAC1 wild-type (WT), S59A and phosphomimetic mutants (6D, 7D and 8D). For each construct, open and closed states are indicated. The conformational state of S59A is based on a known structure (PDB: 7WNQ). b, c Cryo-EM maps of open (teal) and closed (yellow) conformations of AtSLAC1 6D in two views. Densities for each protomer are colored with varying brightness; those for cholesterol hemisuccinate (CHS), detergents and unmodeled regions as gray. Unsharpened maps at a lower contour level (black border lines) show densities of micelle and intracellular regions. Representative 2D class averages in side view are shown. Presence and absence of the connected densities are indicated by filled and empty red triangle, respectively. TMD transmembrane domain, ICD intracellular domain, Ext extracellular side, and Int intracellular side. d, e Open and closed structures of AtSLAC1 6D. Pore helices are colored as teal (open) and yellow (closed); outer helices and loops as cyan (open) and light yellow (closed); and ICL2s as blue. Residue numbers, N- and C-termini are indicated. Disordered regions and ICL2 are represented as dashed lines; membrane bilayers as gray thick lines; pore volumes as blue tubes; and putative chloride ion sites as green spheres. f Conserved sequence motifs nearby ICL2 in dicots, monocots, basal plants, a charophyte Klebsormidium nitens and a liverwort Marchantia polymorpha. Height of each upper-case letter is proportional to conservation level. Blue inverted triangles indicate conserved lysine and arginine sites on ICL2. Sequence alignments were performed by ClustalX54. The plot was prepared using WebLogo55. g I-V relationship of WT ICL2 (KRRLCK) and its mutants in HEK293T cells. h Current densities of WT and its ICL2 mutants in (g) at +60 mV. In (a, g) numbers of observations are indicated in parentheses. Each data was represented as mean ± standard error. One-way ANOVA was used for comparisons against WT with others from Dunnett’s T3 multiple comparisons test. P values are 0.0094, 0.1431, 0.0071, 0.1841, 0.0052, 0.0035 and 0.0030, respectively. Ns not statistically significant; *P ≤  0.05; **P ≤ 0.01.

Back to article page