His-Cys and Trp-Cys cross-links generated by post-translational chemical modification

Figures & data

Figure 1. The structural representation of characteristic amino acids generated by the post-translational modifications from heteroaromatic amino acid side chains.

Figure 2. The superimposed crystal structure of melB pro-tyrosinase with other tyrosinases. (a) whole structure of apo (white, PDB code:3W6Q) and holo form (green, PDB code:3W6W) (b) Copper-binding domains of mushroom (blue, PDB code: 2y9w), plant catechol oxidase (orange, PDB code: 1BT3), and the functional unit g of octopus hemocyanin (pink, PDB code: 1JS8). The protein main chain is displayed as ribbon and key cysteine residues are highlighted as sticks and green sphere indicates copper.

Figure 3. The crystal structure of melB pro-tyrosinase copper-binding site. (a) apo form (b) holo form.

Figure 4. The proposed mechanism of copper incorporation into fungal pro-tyrosinase.

Figure 5. The proposed molecular structure of CTQ-6-oxime in QHNDH.