5E5C

Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1

Summary for 5E5C

• Entry DOI: 10.2210/pdb5e5c/pdb
• Descriptor: D-hydantoinase/dihydropyrimidinase, ZINC ION (3 entities in total)
• Functional Keywords: dihydropyrimidinase, hydrolase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• Total number of polymer chains: 2
• Total formula weight: 106551.07

Authors

Huang, C.C.,Huang, Y.H.,Hsieh, Y.C.,Tzeng, C.T.,Chen, C.J.,Huang, C.Y. (deposition date: 2015-10-08, release date: 2016-09-21, Last modification date: 2023-11-15)

Primary citation

Tzeng, C.T.,Huang, Y.H.,Huang, C.Y.
Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1: Insights into the molecular basis of formation of a dimer
Biochem.Biophys.Res.Commun., 478:1449-1455, 2016

PubMed Abstract: Dihydropyrimidinase, 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 Å resolution. The structure of P. aeruginosa dihydropyrimidinase reveals a classic (β/α)8-barrel structure core embedding the catalytic dimetal center and a β-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.

PubMed: 27576201
DOI: 10.1016/j.bbrc.2016.08.144

Experimental method

X-RAY DIFFRACTION (2.1 Å)