4OQC
Urate OXIDASE CO-CRYSTALLIZED WITH AZIDE
Summary for 4OQC
| Entry DOI | 10.2210/pdb4oqc/pdb |
| Related | 3P9F 3P9O 4FSK 4POE 4PR8 4PUV |
| Descriptor | Uricase, AZIDE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | inhibition, degradation mechanism, peroxisome, purine metabolism, heterotetramer, cofactorless oxidase, oxygen binding |
| Biological source | Aspergillus flavus |
| Cellular location | Peroxisome: Q00511 |
| Total number of polymer chains | 1 |
| Total formula weight | 34290.62 |
| Authors | Colloc'h, N.,Prange, T. (deposition date: 2014-02-08, release date: 2014-12-24, Last modification date: 2024-11-20) |
| Primary citation | Gabison, L.,Colloc'h, N.,Prange, T. Azide inhibition of urate oxidase. Acta Crystallogr.,Sect.F, 70:896-902, 2014 Cited by PubMed Abstract: The inhibition of urate oxidase (UOX) by azide was investigated by X-ray diffraction techniques and compared with cyanide inhibition. Two well characterized sites for reagents are present in the enzyme: the dioxygen site and the substrate-binding site. To examine the selectivity of these sites towards azide inhibition, several crystallization conditions were developed. UOX was co-crystallized with azide (N3) in the presence or absence of either uric acid (UA, the natural substrate) or 8-azaxanthine (8AZA, a competitive inhibitor). In a second set of experiments, previously grown orthorhombic crystals of the UOX-UA or UOX-8AZA complexes were soaked in sodium azide solutions. In a third set of experiments, orthorhombic crystals of UOX with the exchangeable ligand 8-nitroxanthine (8NXN) were soaked in a solution containing uric acid and azide simultaneously (competitive soaking). In all assays, the soaking periods were either short (a few hours) or long (one or two months). These different experimental conditions showed that one or other of the sites, or the two sites together, could be inhibited. This also demonstrated that azide not only competes with dioxygen as cyanide does but also competes with the substrate for its enzymatic site. A model in agreement with experimental data would be an azide in equilibrium between two sites, kinetically in favour of the dioxygen site and thermodynamically in favour of the substrate-binding site. PubMed: 25005084DOI: 10.1107/S2053230X14011753 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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