Structural and Dynamic Requirements for Optimal Activity of the Essential Bacterial Enzyme Dihydrodipicolinate Synthase
Figure 7
Network of essential active site interactions over the course of the simulations.
(A) Electrostatic interactions and residues considered: Wild-type E. coli tetramer (dark blue), E. coli L197 mutant dimer (light blue), MRSA wild-type dimer (green). Only Wild-type E. Coli interactions (dashed lines) are shown for clarity. (B) Distance between T44-Oγ and Y133-Oç. (C) Distance between T44-Oγ and Y107-Oç. (D) Distance between K161-Nζ and Y133-Oç. Equivalent MRSA residues are T46, Y135, Y109 and K163.