1R4U

URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR OXONIC ACID

Summary for 1R4U

• Entry DOI: 10.2210/pdb1r4u/pdb
• Related: 1R4S 1R51 1R56
• Descriptor: Uricase, OXONIC ACID (3 entities in total)
• Functional Keywords: oxidoreductase, uric acid degradation, dimeric barrel, tunnel-shaped protein
• Biological source: Aspergillus flavus
• Cellular location: Peroxisome: Q00511
• Total number of polymer chains: 1
• Total formula weight: 34358.69

Authors

Retailleau, P.,Colloc'h, N.,Prange, T. (deposition date: 2003-10-08, release date: 2004-03-02, Last modification date: 2023-08-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)