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Figure 6
(a) Evolution of the activation level (black curve), the refined occupancy of Cys57 bound to FMN (light gray curve) and the height of the peak corresponding to the adduct in the Fobslight(n) − Fobsdark map (gray) represented as a function of the time delay. (b) Evolution of the RMSD between the dark-state model and the successive light states from 2.5 ms to 92.5 ms after photoactivation (blue to red curves) mapped over the secondary structure representation of CrPhotLOV1. The reactive cysteine (Cys57) is indicated by a star. (c) Heat color cartoon representation of the average RMSD between the dark and light states showing the secondary structures around the C-terminal part that are affected by the adduct formation. The C-terminal linker region with the LOV2 domain present in the full-length phototropin is illustrated with gray dashes connecting an α-helix. (d) Superposition of light states from 2.5 ms (blue) to 92.5 ms after photoactivation (red) over the dark state (gray) with black arrows indicating the directionality of the structural change. |
IUCrJ
ISSN: 2052-2525
BIOLOGY | MEDICINE
Open
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