Figure 4 | Scientific Reports

Figure 4

From: Functional tunability from a distance: Rheostat positions influence allosteric coupling between two distant binding sites

Figure 4

Calculated scores for substituted “distant” positions in and near the allosteric sites of hLPYK. The effects of distant substitutions in the Fru-1,6-BP binding site on Ala binding (Kix-Ala) and PEP/Ala allosteric coupling (Qax-Ala) and the effects of distant substitutions in the Ala binding site on Fru-1,6-BP binding (Kix-FBP) and PEP/Fru-1,6-BP allosteric coupling (Qax-FBP) were used to calculate rheostat (top), neutral (bottom left) and toggle (bottom right) scores for the hLPYK positions noted on the x-axis. The scores for the same variants on their respective “local” parameters were previously reported3. For direct comparison with the distant data and as described in Methods, the revised scores calculated for the local dataset are included in an all-inclusive figure in Supplemental Fig. 6 and Rheoscale scores are reported in Supplemental Table 4 for all positions and all parameters. Dashed vertical lines separate the scores for individual positions. For the rheostat scores, the horizontal dashed line at 0.5 indicates the empirically determined threshold that delineates rheostat positions. For the neutral scores, the horizontal dashed line at 0.7 to delineate high neutral scores is based on empirical comparisons in a previous study19. For the toggle scores, the horizontal dashed line at 0.64 corresponds to the threshold defined in18 to delineate a toggle position.

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