3LD4

Urate oxidase complexed with 8-nitro xanthine

3LD4 の概要

• エントリーDOI: 10.2210/pdb3ld4/pdb
• 関連するPDBエントリー: 1R51 3L8W 3L9G 3LBG
• 分子名称: Uricase, 8-nitro-3,7-dihydro-1H-purine-2,6-dione, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: urate oxidase, aspergillus flavus, nitroxanthine, thioxanthine, xanthine, protonation, peroxisome, purine metabolism, oxidoreductase
• 由来する生物種: Aspergillus flavus
• 細胞内の位置: Peroxisome: Q00511
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33806.92

構造登録者

Prange, T.,Colloc'h, N.,Gabison, L. (登録日: 2010-01-12, 公開日: 2010-06-02, 最終更新日: 2023-11-01)

主引用文献

Gabison, L.,Chiadmi, M.,El Hajji, M.,Castro, B.,Colloc'h, N.,Prange, T.
Near-atomic resolution structures of urate oxidase complexed with its substrate and analogues: the protonation state of the ligand.
Acta Crystallogr.,Sect.D, 66:714-724, 2010

PubMed Abstract: Urate oxidase (uricase; EC 1.7.3.3; UOX) from Aspergillus flavus catalyzes the oxidation of uric acid in the presence of molecular oxygen to 5-hydroxyisourate in the degradation cascade of purines; intriguingly, catalysis proceeds using neither a metal ion (Fe, Cu etc.) nor a redox cofactor. UOX is a tetrameric enzyme with four active sites located at the interface of two subunits; its structure was refined at atomic resolution (1 A) using new crystal data in the presence of xanthine and at near-atomic resolution (1.3-1.7 A) in complexes with the natural substrate (urate) and two inhibitors: 8-nitroxanthine and 8-thiouric acid. Three new features of the structural and mechanistic behaviour of the enzyme were addressed. Firstly, the high resolution of the UOX-xanthine structure allowed the solution of an old structural problem at a contact zone within the tetramer; secondly, the protonation state of the substrate was determined from both a halochromic inhibitor complex (UOX-8-nitroxanthine) and from the H-atom distribution in the active site, using the structures of the UOX-xanthine and the UOX-uric acid complexes; and thirdly, it was possible to extend the general base system, characterized by the conserved catalytic triad Thr-Lys-His, to a large water network that is able to buffer and shuttle protons back and forth between the substrate and the peroxo hole along the reaction pathway.

PubMed: 20516624
DOI: 10.1107/S090744491001142X

実験手法

X-RAY DIFFRACTION (1.35 Å)