Figure 4 - full size

Figure 4.
(a) The HMP-P synthase homodimer. The protomer consists of three domains. The N-terminal domains are colored in shades of blue, the ( )[8] core domains are colored in shades of green and the C-terminal domains are colored in shades of red. HMP-P is shown as a ball-and-stick model. The final 66 amino acids are disordered; however, the final ordered residues, which immediately precede a conserved CX[2]CX[4]C motif, extend into the active site of the adjacent protomer. The C-terminal tail is anchored to the adjacent protomer by a three-helix bundle motif located at the beginning of the C-terminal domain. (b) Stereoview of the HMP-P synthase active site with modeled SAM and the [4Fe-4S] cluster. The atoms are color coded by atom type (green = C, blue = N, red = O, yellow = S and orange = Fe). The substrate analog IMR 22 from the crystal structure is shown. Residues Cys561, Cys564 and Cys569, SAM and the [4Fe-4S] cluster were modeled using biotin synthase as a guide. Hydrogen bonds are indicated by dotted lines. (c) Superposition of the ( )[8] domains from HMP-P synthase and biotin synthase (PDB ID 1R3O). HMP-P synthase is shown in blue, and biotin synthase is shown in silver. The [4Fe-4S] cluster and SAM from biotin synthase are shown as ball-and-stick models.