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Dynamic Allostery in the Methionine Repressor Revealed by Force Distribution Analysis

Figure 6

Differences between SAM and SAH.

(A) Changes in residue-wise forces for MetJ-dna when replacing SAM by SAH. As expected, the strongest differences are observed for residues in close proximity to the charged sulfur atom. (B) Increased quenching of dynamics upon SAM binding. Plotted are differences in backbone RMSF for MetJ-dna in complex with SAM and SAH along the protein sequence for both monomers (red and blue). Positive values indicate increased stiffening for MetJ-SAM. The secondary structure is marked in gray. (C) Difference in residue wise forces for MetJ-dna when substituting SAM by SAH for both monomers (red and blue). The secondary structure is marked in gray. Tyr11 and Ile28 (marked with arrows) show a high in the second monomer for which the DNA is fully resolved in the crystal structure.

doi: https://doi.org/10.1371/journal.pcbi.1000574.g006