3OBP
Anaerobic complex of urate oxidase with uric acid
Summary for 3OBP
| Entry DOI | 10.2210/pdb3obp/pdb |
| Related | 1R4S 3BJP |
| Descriptor | Uricase, URIC ACID, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | uric acid, inhibition, degradation mechanism, oxidoreductase, peroxisome, purine metabolism |
| Biological source | Aspergillus flavus |
| Cellular location | Peroxisome: Q00511 |
| Total number of polymer chains | 1 |
| Total formula weight | 34374.69 |
| Authors | Gabison, L.,Chopard, C.,Colloc'h, N.,El Hajji, M.,Castro, B.,Chiadmi, M.,Prange, T. (deposition date: 2010-08-08, release date: 2011-06-22, Last modification date: 2024-10-16) |
| Primary citation | Gabison, L.,Chopard, C.,Colloc'h, N.,Peyrot, F.,Castro, B.,Hajji, M.E.,Altarsha, M.,Monard, G.,Chiadmi, M.,Prange, T. X-ray, ESR, and quantum mechanics studies unravel a spin well in the cofactor-less urate oxidase. Proteins, 79:1964-1976, 2011 Cited by PubMed Abstract: Urate oxidase (EC 1.7.3.3 or UOX) catalyzes the conversion of uric acid using gaseous molecular oxygen to 5-hydroxyisourate and hydrogen peroxide in absence of any cofactor or transition metal. The catalytic mechanism was investigated using X-ray diffraction, electron spin resonance spectroscopy (ESR), and quantum mechanics calculations. The X-ray structure of the anaerobic enzyme-substrate complex gives credit to substrate activation before the dioxygen fixation in the peroxo hole, where incoming and outgoing reagents (dioxygen, water, and hydrogen peroxide molecules) are handled. ESR spectroscopy establishes the initial monoelectron activation of the substrate without the participation of dioxygen. In addition, both X-ray structure and quantum mechanic calculations promote a conserved base oxidative system as the main structural features in UOX that protonates/deprotonates and activate the substrate into the doublet state now able to satisfy the Wigner's spin selection rule for reaction with molecular oxygen in its triplet ground state. PubMed: 21491497DOI: 10.1002/prot.23022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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