Fig. 3: Structure comparison of closed, non-conducting state 1, non-conducting state 2, and conducting state of dimeric OSCA1.1.

a Top view of closed OSCA1.1 colored in purple is shown as a cartoon. Helices are shown as cylinders and the interface lipid in the central cavity is shown as spheres. The 11 transmembrane helices M0 to M10 are labeled. b–d Top view of OSCA1.1-F516A in non-conducting state 1 (b, brown), non-conducting state 2 (c, pink), and conducting state (d, cyan). e Superimposed top view of the transmembrane layer cross-section of wildtype OSCA1.1 in closed state (purple) and OSCA1.1-F516A in non-conducting state 1 (brown). The 11 transmembrane helices M0 to M10 are labeled and linked by a dashed curve in color following the same scheme used in transmembrane helices. The interface lipid is shown as a wavy line. The transmembrane helices exhibit a counterclockwise rotation from closed state to non-conducting state 1. M3 and M10 helices in closed state and non-conducting state 1 are linked by black lines and red lines, respectively. f Superimposed top view of the transmembrane layer cross-section of OSCA1.1-F516A in non-conducting state 1 (brown) and OSCA1.1-F516A in non-conducting state 2 (pink). M3 and M10 helices in non-conducting state 1 and non-conducting state 2 are linked by black lines and red lines, respectively. g Superimposed top view of the transmembrane layer cross-section of OSCA1.1-F516A in non-conducting state 2 (pink) and OSCA1.1-F516A in conducting state (blue). M3 and M10 helices in non-conducting state 2 and conducting state are linked by black lines and red lines, respectively. The interface lipids tended to dissociate from the central cavity in the OSCA1.1-F516A conducting state. h Superimposed top view of the transmembrane layer cross-section of wildtype OSCA1.1 in closed state (purple) and OSCA1.1-F516A in conducting state (blue). M3 and M10 helices in the closed state and conducting state are linked by black lines and red lines, respectively.