Dynamic Regulation of Phenylalanine Hydroxylase by Simulated Redox Manipulation
Figure 5
Alteration in local dynamics in phenylalanine hydroxylase upon side chain oxidation.
Residue-wise B-factors for the 2*16 REMD trajectories were calculated for Cα-atoms and compared between simulations of equal temperatures. Rank-based differences were mapped on the protein structure, where blue regions indicate regions more flexible in more of the 16 simulations of PAHnat. Unaffected regions are shown in white, whereas red regions indicate regions showing elevated backbone dynamics in more of the 16 simulations of PAHox. Elevated B-factors in the central helices suggest an allosteric signal transduction over this path from the introduced oxidation site (Cys203, Cys334) to the Tyr138-loop near the catalytic center. The bottom picture shows the same structure rotated by 220° to highlight local effects on the oxidation site in the back of the top picture.