4N9M
Joint neutron/x-ray structure of urate oxidase in complex with 8-hydroxyxanthine
Summary for 4N9M
| Entry DOI | 10.2210/pdb4n9m/pdb |
| Related | 3L9G 4N3M 4N9S 4N9V |
| Descriptor | Uricase, 8-hydroxy-3,9-dihydro-1H-purine-2,6-dione, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | urate oxidase, uricase oxidoreductase, oxidoreductase |
| Biological source | Aspergillus flavus |
| Total number of polymer chains | 1 |
| Total formula weight | 34410.14 |
| Authors | Oksanen, E.,Blakeley, M.P.,Budayova-Spano, M. (deposition date: 2013-10-21, release date: 2014-02-05, Last modification date: 2024-11-20) |
| Primary citation | Oksanen, E.,Blakeley, M.P.,El-Hajji, M.,Ryde, U.,Budayova-Spano, M. The neutron structure of urate oxidase resolves a long-standing mechanistic conundrum and reveals unexpected changes in protonation. Plos One, 9:e86651-e86651, 2014 Cited by PubMed Abstract: Urate oxidase transforms uric acid to 5-hydroxyisourate without the help of cofactors, but the catalytic mechanism has remained enigmatic, as the protonation state of the substrate could not be reliably deduced. We have determined the neutron structure of urate oxidase, providing unique information on the proton positions. A neutron crystal structure inhibited by a chloride anion at 2.3 Å resolution shows that the substrate is in fact 8-hydroxyxanthine, the enol tautomer of urate. We have also determined the neutron structure of the complex with the inhibitor 8-azaxanthine at 1.9 Å resolution, showing the protonation states of the K10-T57-H256 catalytic triad. Together with X-ray data and quantum chemical calculations, these structures allow us to identify the site of the initial substrate protonation and elucidate why the enzyme is inhibited by a chloride anion. PubMed: 24466188DOI: 10.1371/journal.pone.0086651 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.298 Å) X-RAY DIFFRACTION (2.023 Å) |
Structure validation
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