Figure 4 - full size


Figure 4.
FIG. 4. Comparison of the monomer structures and the putative catalytic sites between DJ-1 and protease I. Ribbon diagrams of the monomer subunits of DJ-1 (a) and protease I (b). Secondary structure is color-coded as in Fig. 2a. c, the region around the putative active site of DJ-1 including 5, 5, and the nucleophile elbow in monomer A (in blue) and 8 and 9 in monomer B (in green). The residues Cys-106, His-126, and Val-128 in monomer A and Leu-166, Val-181, Lys-182, Pro-184 (a backbone oxygen), Val-186, and Leu-187 in monomer B are shown as ball-and-stick models. The His-126 imidazole ring forms hydrogen bonds with the main-chain carbonyl group of Pro-184 (monomer B) and the main-chain amide group of Val-128 (monomer A) are shown by the dotted lines. Thus, the His-126 imidazole ring does not take a preferable orientation for protease activity. Leu-166, mutated to proline in PARK7 patients, is shown in red. d, the region around the active site of protease I including the nucleophile elbow in which the catalytic residue Cys-100 is located. Protease I forms a hexamer, and the catalytic triad is formed in the dimer interface (monomer A is in blue, and monomer B is in green).

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 31380-31384) copyright 2003.