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. 2012 Feb 16;7(2):e31133. doi: 10.1371/journal.pone.0031133

Figure 8. Structural basis of inhibition by D-2-aminopimelate.

Figure 8

A. Composite stereo view of the active site of PaDapD with bound succinamide-CoA, and the substrate L-2-AP. The position of the inactive substrate analogue succinamide-CoA (orange) and the L-2-aminopimelate (yellow) bound in the ternary complex were derived from a superposition with the DapD-succinamide-CoA-L-2AP complex (1KGQ). The bound L-2AP in the PaDapD-L-2AP complex is shown in blue. B. View of a composite model of the catalytically incompetent complex of PaDapD with bound succinamide-CoA, and the inhibitor D-2AP. The model was created using the same templates as in (A), the bound D-2AP in the structure of the complex of PaDaD with this ligand is shown in green.