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5YKD

Crystal structure of dihydropyrimidinase from Pseudomonas aeruginosa PAO1 at 2.17 angstrom resolution

5YKD の概要
エントリーDOI10.2210/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
Huang, Y.H.,Huang, C.Y. (登録日: 2017-10-14, 公開日: 2018-02-21, 最終更新日: 2023-11-22)
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: 29666631
DOI: 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)
構造検証レポート
Validation report summary of 5ykd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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