4D17
Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 106 kGy)
Summary for 4D17
| Entry DOI | 10.2210/pdb4d17/pdb |
| Related | 4D12 4D13 4D19 |
| Descriptor | URICASE, 5-(HYDRO)PEROXOISOURATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, cofactor-free oxidase |
| Biological source | ASPERGILLUS FLAVUS |
| Cellular location | Peroxisome: Q00511 |
| Total number of polymer chains | 1 |
| Total formula weight | 34807.13 |
| Authors | Bui, S.,Steiner, R.A. (deposition date: 2014-05-01, release date: 2014-11-05, Last modification date: 2024-05-08) |
| Primary citation | Bui, S.,von Stetten, D.,Jambrina, P.G.,Prange, T.,Colloc'h, N.,de Sanctis, D.,Royant, A.,Rosta, E.,Steiner, R.A. Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase. Angew. Chem. Int. Ed. Engl., 53:13710-13714, 2014 Cited by PubMed Abstract: Cofactor-free oxidases and oxygenases promote and control the reactivity of O2 with limited chemical tools at their disposal. Their mechanism of action is not completely understood and structural information is not available for any of the reaction intermediates. Near-atomic resolution crystallography supported by in crystallo Raman spectroscopy and QM/MM calculations showed unambiguously that the archetypical cofactor-free uricase catalyzes uric acid degradation via a C5(S)-(hydro)peroxide intermediate. Low X-ray doses break specifically the intermediate C5-OO(H) bond at 100 K, thus releasing O2 in situ, which is trapped above the substrate radical. The dose-dependent rate of bond rupture followed by combined crystallographic and Raman analysis indicates that ionizing radiation kick-starts both peroxide decomposition and its regeneration. Peroxidation can be explained by a mechanism in which the substrate radical recombines with superoxide transiently produced in the active site. PubMed: 25314114DOI: 10.1002/anie.201405485 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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