Structural and Dynamic Requirements for Optimal Activity of the Essential Bacterial Enzyme Dihydrodipicolinate Synthase
Figure 2
Overall simulations results for E. coli DHDPS tetramer and dimer.
(A) Cα RMSDs over the course of the simulations, for dimers from tet-1 & tet-2 (shades of grey), dim-A (blue), dim-B (light blue); (B) Cartoon representation of monomer-monomer reorientation during simulation of dimers. The relative rotation of monomers is represented by dotted lines and an arrow. Cartoons are shown for extreme conformations taken from dim-B (light-blue at 70 ns, blue at 433 ns), and mrsa-1 (green at 430 ns). Cα RMSD between extreme conformations are: 4.0 Å for the E.coli and 3.8 Å for the MRSA dimers. (C) Cα RMSD values for monomers from tet-1 & tet-2 (shades of grey), dim-A & dim-B (shades of blue); (D) Angles of rotation corresponding to monomer rearrangement. Only tet1-A (black), dim-A (blue) and dim-B (light blue) are represented for clarity, the thick lines represent the spline fit of the values.