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. Author manuscript; available in PMC: 2019 Mar 25.
Published in final edited form as: Sci Signal. 2017 Nov 28;10(507):eaao0358. doi: 10.1126/scisignal.aao0358

Figure 6. Side-chain twist of the Arg91 gate induced by constitutively-active Orai1-H134A channels.

Figure 6

(A,B) Representative snap shot of the equilibrated part of the 200-ns-long molecular dynamics simulations for wild-type Orai1 (A) and Orai1-H134A (B) showing the position of Arg91 residues and Ser90 in the TM1 helices, which are surrounded by TM2 helices (His134 or Ala134 respectively shown) from a top view. (C, D) Hydrogen bonds between Arg91 and Ser90 in wild-type Orai1 (C) and the Orai1-H134A simulations (D) in a time-course (150 to 200 ns). (E,F) Comparison of pore surfaces of wild-type Orai1 (E) and Orai1-H134A (F) before and after Ca2+ is pulled through the pore. The pore surface is shown in blue (radius > 1.15Å) and green (radius is between 0.6 to 1.15Å). (G,H) Representative snap shots of the start and end of 200-ns-long molecular dynamics simulations for wild-type Orai1 (G) and Orai1-H134A (H) illustrates the position of Phe99 residues in the pore helix.