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. Author manuscript; available in PMC: 2022 May 23.
Published in final edited form as: Cell. 2022 Feb 2;185(4):672–689.e23. doi: 10.1016/j.cell.2022.01.007

Figure 4. The functional importance of trimeric assembly.

Figure 4

(A and B) The opening within the trimer interface in ChRmine (left) and HsBR (right). Opening: gray (A). Electrostatic potential surface (B).

(C) Trimer opening radii of the ChRmine.

(D) Magnified views of the blue-boxed region from (A), the constriction formed by ECL1, from two angles.

(E and F) Magnified views of the green- and orange-boxed regions in (A), the H-bond interactions between protomers at the intracellular (E) and extracellular

(F) side.

(G) FSEC traces of ChRmine WT, S138W, Y156F, and S138W/Y156F mutants.

(H) Photocurrent amplitudes for the mutants shown in (E) and (F), as well as R136H (negative control) (n = 4−7).

(I) Reversal potentials of ChRmine WT, R136H, and S138W mutants (n = 3–9). All data mean ± SEM; sample size n denotes the number of cells. One-way ANOVA with Dunnett’s test (I) and unpaired t test (H), **p < 0.01 and ****p < 0.0001. N.S., not significant.