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Dihydropyrimidinase, a dimetalloenzyme containing a carboxylated lysine within the active site, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH. In this paper, we report the crystal structure of  P. aeruginosa  dihydropyrimidinase at pH 5.9 (PDB entry 5YKD). The crystals of  P. aeruginosa  dihydropyrimidinase belonged to space group  C 222 1  with cell dimensions of  a  = 108.9,  b  = 155.7, and  c  = 235.6 Å. The structure of  P. aeruginosa  dihydropyrimidinase was solved at 2.17 Å resolution. An asymmetric unit of the crystal contained four crystallographically independent  P. aeruginosa  dihydropyrimidinase monomers. Gel filtration chromatographic analysis of purified  P. aeruginosa  dihydropyrimidinase revealed a mixture of dimers and tetramers at pH 5.9. Thus,  P. aeruginosa  dihydropyrimidinase can form a stable tetramer both in the crystalline state and in the solution. Based on sequence analysis and structural comparison of the dimer-dimer interface between  P. aeruginosa  dihydropyrimidinase and  Thermus  sp. dihydropyrimidinase, different oligomerization mechanisms are proposed.

Structural Basis for pH-Dependent Oligomerization of Dihydropyrimidinase fromPseudomonas aeruginosaPAO1