Fig. 9.

Comparison of the model of CFTR conformer 2 (closed channel, 30 ns) and the experimental 3D structure of N. aromaticivorans Atm1 (inward-facing conformation). Amino acids from the 12 transmembrane helices (TM) included in the membrane space were superimposed (114 Cα atoms, RMSD 2.55 Å). The coordinates of the N. aromaticivorans Atm1 were taken from pdb:4mrs (2.35 Å resolution). A Lateral views of the MSD1 block 2 (green) and MSD2 block 4 (red). CFTR and Atm1 ribbons are colored dark and light, respectively. Two amino acids that are very close to each other in TM6 and TM12 are shown at right (V302 (pink and green) for Atm1, F337 and G1130 for CFTR, also see Online Resource 29). B A view of the superimposition from the extracellular side, focusing at the level of the tight closure of the channel [as observed in Atm1 (pink and green) and predicted for CFTR (F337 and G1130)]