4OP6
Urate OXIDASE + 8-AZAXANTHINE UNDER 40 BARS OXYGEN
Summary for 4OP6
| Entry DOI | 10.2210/pdb4op6/pdb |
| Related | 4op9 |
| Descriptor | Uricase, 8-AZAXANTHINE, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | homotetramer, t-fold domain, purine metabolism, oxidoreductase, oxygen binding, uric acid, peroxisome |
| Biological source | Aspergillus flavus |
| Total number of polymer chains | 1 |
| Total formula weight | 34391.68 |
| Authors | Colloc'h, N.,Prange, T. (deposition date: 2014-02-05, release date: 2014-03-19, Last modification date: 2023-11-08) |
| Primary citation | Colloc'h, N.,Prange, T. Functional relevance of the internal hydrophobic cavity of urate oxidase. Febs Lett., 588:1715-1719, 2014 Cited by PubMed Abstract: Urate oxidase from Aspergillus flavus is a 135 kDa homo-tetramer which has a hydrophobic cavity buried within each monomer and located close to its active site. Crystallographic studies under moderate gas pressure and high hydrostatic pressure have shown that both gas presence and high pressure would rigidify the cavity leading to an inhibition of the catalytic activity. Analysis of the cavity volume variations and functional modifications suggest that the flexibility of the cavity would be an essential parameter for the active site efficiency. This cavity would act as a connecting vessel to give flexibility to the neighboring active site, and its expansion under pure oxygen pressure reveals that it might serve as a transient reservoir on its pathway to the active site. PubMed: 24657440DOI: 10.1016/j.febslet.2014.03.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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