4puv | pdb_00004puv

URATE OXIDASE DI-AZIDE complex

spinqualitylabelsall models 4puv, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4puv is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACE, AZI, NA Related: 4pr8, 4poe, 4oqc, 3p9f Activity: Factor independent urate hydroxylase, with EC number 1.7.3.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. Publication Abstract from PubMed 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. Azide inhibition of urate oxidase.,Gabison L, Colloc'h N, Prange T Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):896-902. doi:, 10.1107/S2053230X14011753. Epub 2014 Jun 18. PMID:25005084 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urate Oxidase

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