Fig. 1: Structure of HeR 48C12.
a The overall structure of HeR. For comparison, the HeR structure is superimposed onto the BR structure (1C3W). b The overall dimer structure of HeR. c The electrostatic surface view of HeR. Red and blue correspond to potentials of −5 kT e−1 and 5 kT e−1, respectively. d The ATR core of HeR and BR (1C3W). e Structural comparison of the proton pumping chain of BR (1C3W) with the corresponding region in HeR. The magenta cross indicates that the proton pumping path is blocked in HeR. f Structural comparison of HeR with channelrhodopsin C1C2 (3UG9) in the potential ‘channel’ region. The negatively charged residues distributed in the tunnel formed by TM1, 2, 3 and 7 of channelrhodopsin C1C2 are marked in red, while the hydrophobic residues localized in the counterpart region of HeR are marked in brown gold.
