4YSK
Crystal structure of apo-form SdoA from Pseudomonas putida
4YSK の概要
エントリーDOI | 10.2210/pdb4ysk/pdb |
分子名称 | Beta-lactamase domain protein, FE (III) ION (3 entities in total) |
機能のキーワード | sulfur dioxygenase, persulfide dioxygenase, sdoa, hydrolase |
由来する生物種 | Pseudomonas putida (strain F1 / ATCC 700007) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 65471.70 |
構造登録者 | Sattler, S.A.,Wang, X.,DeHan, P.J.,Xun, L.,Kang, C. (登録日: 2015-03-17, 公開日: 2015-06-24, 最終更新日: 2024-02-28) |
主引用文献 | Sattler, S.A.,Wang, X.,Lewis, K.M.,DeHan, P.J.,Park, C.M.,Xin, Y.,Liu, H.,Xian, M.,Xun, L.,Kang, C. Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-beta-lactamase Superfamily. J.Biol.Chem., 290:18914-18923, 2015 Cited by PubMed Abstract: Persulfide dioxygenases (PDOs), also known as sulfur dioxygenases (SDOs), oxidize glutathione persulfide (GSSH) to sulfite and GSH. PDOs belong to the metallo-β-lactamase superfamily and play critical roles in animals, plants, and microorganisms, including sulfide detoxification. The structures of two PDOs from human and Arabidopsis thaliana have been reported; however, little is known about the substrate binding and catalytic mechanism. The crystal structures of two bacterial PDOs from Pseudomonas putida and Myxococcus xanthus were determined at 1.5- and 2.5-Å resolution, respectively. The structures of both PDOs were homodimers, and their metal centers and β-lactamase folds were superimposable with those of related enzymes, especially the glyoxalases II. The PDOs share similar Fe(II) coordination and a secondary coordination sphere-based hydrogen bond network that is absent in glyoxalases II, in which the corresponding residues are involved instead in coordinating a second metal ion. The crystal structure of the complex between the Pseudomonas PDO and GSH also reveals the similarity of substrate binding between it and glyoxalases II. Further analysis implicates an identical mode of substrate binding by known PDOs. Thus, the data not only reveal the differences in metal binding and coordination between the dioxygenases and the hydrolytic enzymes in the metallo-β-lactamase superfamily, but also provide detailed information on substrate binding by PDOs. PubMed: 26082492DOI: 10.1074/jbc.M115.652537 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.466 Å) |
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