5YKD
Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1 at 2.17 angstrom resolution
5YKD の概要
| エントリーDOI | 10.2210/pdb5ykd/pdb |
| 分子名称 | D-hydantoinase/dihydropyrimidinase, ZINC ION (3 entities in total) |
| 機能のキーワード | dihydropyrimidinase, hydrolase |
| 由来する生物種 | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 209786.65 |
| 構造登録者 | |
| 主引用文献 | Cheng, J.H.,Huang, C.C.,Huang, Y.H.,Huang, C.Y. Structural Basis for pH-Dependent Oligomerization of Dihydropyrimidinase fromPseudomonas aeruginosaPAO1. Bioinorg Chem Appl, 2018:9564391-9564391, 2018 Cited by PubMed Abstract: 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 dihydropyrimidinase at pH 5.9 (PDB entry 5YKD). The crystals of dihydropyrimidinase belonged to space group 222 with cell dimensions of = 108.9, = 155.7, and = 235.6 Å. The structure of dihydropyrimidinase was solved at 2.17 Å resolution. An asymmetric unit of the crystal contained four crystallographically independent dihydropyrimidinase monomers. Gel filtration chromatographic analysis of purified dihydropyrimidinase revealed a mixture of dimers and tetramers at pH 5.9. Thus, 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 dihydropyrimidinase and sp. dihydropyrimidinase, different oligomerization mechanisms are proposed. PubMed: 29666631DOI: 10.1155/2018/9564391 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.17 Å) |
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