Fig. 2: Comparison of the HcKCR1_C110A and wild-type HcKCR1 (PDB: 8GI8) dark-adapted structures and functional characterization of C110 mutants.
From: Structural insights into light-gating of potassium-selective channelrhodopsin
a An overlay of structures of dark-adapted C110A mutant (shown in blue, retinal in yellow) and wild-type (WT, shown in gray). The helices are shown as cartoons, the chromophore and the residue 110 side chains, as sticks. b A zoom-in into the residue 110 region. c Representative photocurrent traces recorded at 0 mV in response to 200-ms light pulses (green bar) normalized at the peak value. d, e Photocurrent rise and decay time constants. The symbols are individual-cell data; the lines are mean ± sem values. *p = 3.7E-4 (n = 10, 26, and 23 cells for the WT, C110A, and C110T, respectively); **p = 4.3E-5 (n = 16, 10, and 17 cells for the WT, C110A, and C110T, respectively) by the two-tailed Mann–Whitney test. f Current-voltage dependencies (mean ± sem, n = 25, 37, and 40 cells for the WT, C110A, and C110T, respectively). Source data are provided as a Source Data file.
