Figure 3.

Co-complex structure of n-MmA:aaPGT. a) The overall co-complex structure of n-MmA:aaPGT in a ribbon representation. The protein structure is shown in gray with the five conserved motifs that typify PGTs colored in red, yellow, blue, green and purple, and the flexible loop region colored in pink with a dashed line representing the missing residues. n-MmA is shown in stick and ball (carbon, yellow; oxygen, red; nitrogen, blue; phosphate, orange). b) A comparison of the conformations of helix 3, 4 and the coil between apo-enzyme (light blue) and complex structure (brown) of aaPGT (left) and saPGT (right). c) A close-up view of the electron density maps (pink: 1σ 2fo-fc for the protein; blue: 1σ omit 2fo-fc map calculated using the final protein structure annealed at 3000K in the absence of the ligand) at the n-MmA binding site (the structure is rotated from that in Figure 3a for a better presentation). The protein is shown in sticks (carbon, white; oxygen, red; nitrogen, blue) with its map colored in pink; n-MmA is also shown in sticks with its map colored in blue. The figures are made in Pymol.