5e5c
From Proteopedia
Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1
Structural highlights
FunctionHYDA_PSEAE Catalyzes the hydrolysis of dihydropyrimidines and of the structurally related DL-5-mono-substituted hydantoins, to produce N-carbamoyl-D-amino acids. Publication Abstract from PubMedDihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. In this paper, we report the crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1 at 2.1 A resolution. The structure of P. aeruginosa dihydropyrimidinase reveals a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a beta-sandwich domain, which is commonly found in the architecture of dihydropyrimidinases. In contrast to all dihydropyrimidinases, P. aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Basing on sequence analysis and structural comparison of the C-terminal region and the dimer-dimer interface between P. aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase, we propose a working model to explain why this enzyme cannot be a tetramer. Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1: Insights into the molecular basis of formation of a dimer.,Tzeng CT, Huang YH, Huang CY Biochem Biophys Res Commun. 2016 Sep 23;478(3):1449-55. doi:, 10.1016/j.bbrc.2016.08.144. Epub 2016 Aug 26. PMID:27576201[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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