3F2M
Urate oxidase complexed with 8-azaxanthine at 150 MPa
Summary for 3F2M
| Entry DOI | 10.2210/pdb3f2m/pdb |
| Descriptor | Uricase, 8-AZAXANTHINE, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | high pressure, uric acid degradation, tetramer, t-fold domain, peroxisome, purine metabolism, oxidoreductase, hpmx |
| Biological source | Aspergillus flavus |
| Cellular location | Peroxisome: Q00511 |
| Total number of polymer chains | 1 |
| Total formula weight | 34359.68 |
| Authors | Colloc'h, N.,Girard, E.,Kahn, R.,Fourme, R. (deposition date: 2008-10-30, release date: 2009-11-10, Last modification date: 2024-10-30) |
| Primary citation | Girard, E.,Marchal, S.,Perez, J.,Finet, S.,Kahn, R.,Fourme, R.,Marassio, G.,Dhaussy, A.C.,Prange, T.,Giffard, M.,Dulin, F.,Bonnete, F.,Lange, R.,Abraini, J.H.,Mezouar, M.,Colloc'h, N. Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure. Biophys.J., 98:2365-2373, 2010 Cited by PubMed Abstract: 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. PubMed: 20483346DOI: 10.1016/j.bpj.2010.01.058 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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