3f2m | pdb_00003f2m

Urate oxidase complexed with 8-azaxanthine at 150 MPa

spinqualitylabelsall models 3f2m, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f2m is a 1 chain structure with sequence from Aspfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZA, NA NonStd Res: ACE Gene: uaZ, uox (ASPFL) 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Structure-function relationships in the tetrameric enzyme urate oxidase were investigated using pressure perturbation. As the active sites are located at the interfaces between monomers, enzyme activity is directly related to the integrity of the tetramer. The effect of hydrostatic pressure on the enzyme was investigated by x-ray crystallography, small-angle x-ray scattering, and fluorescence spectroscopy. Enzymatic activity was also measured under pressure and after decompression. A global model, consistent with all measurements, discloses structural and functional details of the pressure-induced dissociation of the tetramer. Before dissociating, the pressurized protein adopts a conformational substate characterized by an expansion of its substrate binding pocket at the expense of a large neighboring hydrophobic cavity. This substate should be adopted by the enzyme during its catalytic mechanism, where the active site has to accommodate larger intermediates and product. The approach, combining several high-pressure techniques, offers a new (to our knowledge) means of exploring structural and functional properties of transient states relevant to protein mechanisms. Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure.,Girard E, Marchal S, Perez J, Finet S, Kahn R, Fourme R, Marassio G, Dhaussy AC, Prange T, Giffard M, Dulin F, Bonnete F, Lange R, Abraini JH, Mezouar M, Colloc'h N Biophys J. 2010 May 19;98(10):2365-73. doi: 10.1016/j.bpj.2010.01.058. PMID:20483346 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urate Oxidase

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