Structural and Dynamic Requirements for Optimal Activity of the Essential Bacterial Enzyme Dihydrodipicolinate Synthase
Figure 3
Flexibility and stereochemistry of active sites in E. coli DHDPS tetramer and dimer simulations.
(A) RMSDs of active site residues for E. coli tetramers and dimers: tet-1 & tet-2 (grey shades, 8 curves overlayed for 2×4 active sites), dim-A (light blue, 2 curves), dim-B (dark blue, 2 curves). (B) Individual RMSFs of active site residues, averaged over all simulations, with error bars: tet-1 and tet-2 (grey, 2×4 active sites), dim-A and dim-B (blue, 2×2 active sites), mrsa-1 and mrsa-2 (green, 2×2 active sites; E. coli numbering). (C) and (D) Ramachandran plots of the Y107 backbone dihedral angles in the E. coli tetramer and dimer simulations, respectively. Red crosses indicate the crystallographic geometries. The orange contour map (or “favoured” region) accounts for 98% of the phi-psi angles analysed by Lovell et al [25]. Pale orange contour maps account for 99.95% (“allowed”). Percentages represent the time spent in the 3 regions of the plot.