Structural Basis for pH-Dependent Oligomerization of Dihydropyrimidinase from Pseudomonas aeruginosa PAO1

Figure 3

Structural comparison. (a) Superposition of the active site of dihydropyrimidinases. Their active sites contain four histidines, one aspartate, and one carboxylated lysine residue, which are required for metal binding and catalytic activity. Dihydropyrimidinases from P. aeruginosa (PDB entry 5E5C; green), Thermus sp. (PDB entry 1GKQ; salmon), Tetraodon nigroviridis (PDB entry 4H01; pale yellow), and the structure (PDB entry 5YKD; purple blue) in this study are shown. The architecture of these active sites is similar. (b) Superposition of the active site of members of the amidohydrolase family. Their active sites contain four histidines, one aspartate, and one carboxylated lysine residue, which are required for metal binding and catalytic activity. P. aeruginosa dihydropyrimidinase (PDB entry 5YKD; purple blue), Escherichia coli allantoinase (PDB entry 3E74; bright orange), Burkholderia pickettii hydantoinase (PDB entry 1NFG; aquamarine), and E. coli dihydroorotase (PDB entry 1J79; brown) are shown. The architecture of these active sites is similar.

(a)

(b)