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Structural basis of pH dependent oligomerization of dihydropyrimidinase from Pseudomonas aeruginosa pao1

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Document pages: 8 pages

Abstract: Dihydropyrimidinase is a dimeric metalloenzyme containing carboxylated lysine in the active site. It is a member of the cyclic aminohydrolase family, which also includes allantoinase, dihydrolactase, hydantoinase and imidazole enzymes. Unlike all known tetrameric dihydropyrimidinases, Pseudomonas dihydropyrimidinases form dimers at neutral pH. In this paper, we report the crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa at pH 5.9 (PDB entry 5ykd). The crystal of Pseudomonas aeruginosa dihydropyrimidinase belongs to space group C2221, and the cell sizes are a   =   108.9, B   =   155.7 and C   =   235.6   197. The structure of Pseudomonas aeruginosa dihydropyrimidinase is analyzed as 2.17   197; resolution. An asymmetric crystal unit contains four crystal independent Pseudomonas aeruginosa dihydropyrimidinase Mnomers. 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.

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