1R56

UNCOMPLEXED URATE OXIDASE FROM ASPERGILLUS FLAVUS

1R56 の概要

• エントリーDOI: 10.2210/pdb1r56/pdb
• 関連するPDBエントリー: 1R4S 1R4U 1R51 1UOX
• 分子名称: Uricase, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: oxidoreductase, uric acid degradation, dimeric barrel, tunnel-shaped protein
• 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: 8
• 化学式量合計: 273808.93

構造登録者

Retailleau, P.,Colloc'h, N.,Prange, T. (登録日: 2003-10-09, 公開日: 2004-03-02, 最終更新日: 2023-08-23)

主引用文献

Retailleau, P.,Colloc'h, N.,Vivares, D.,Bonnete, F.,Castro, B.,El-Hajji, M.,Mornon, J.P.,Monard, G.,Prange, T.
Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode.
Acta Crystallogr.,Sect.D, 60:453-462, 2004

PubMed Abstract: High-resolution X-ray structures of the complexes of Aspergillus flavus urate oxidase (Uox) with three inhibitors, 8-azaxanthin (AZA), 9-methyl uric acid (MUA) and oxonic acid (OXC), were determined in an orthorhombic space group (I222). In addition, the ligand-free enzyme was also crystallized in a monoclinic form (P2(1)) and its structure determined. Higher accuracy in the three new enzyme-inhibitor complex structures (Uox-AZA, Uox-MUA and Uox-OXC) with respect to the previously determined structure of Uox-AZA (PDB code 1uox) leads to a reversed position of the inhibitor in the active site of the enzyme. The corrected anchoring of the substrate (uric acid) allows an improvement in the understanding of the enzymatic mechanism of urate oxidase.

PubMed: 14993669
DOI: 10.1107/S0907444903029718

実験手法

X-RAY DIFFRACTION (2.3 Å)