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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution.

The gene coding for urate oxidase, an enzyme that catalyzes the oxidation of uric acid to allantoin, is inactivated in humans. Consequently, urate oxidase is used as a protein drug to overcome severe disorders induced by uric acid accumulation. The structure of the active homotetrameric enzyme reveals the existence of a small architectural domain that we call T-fold (for tunnelling-fold) domain. It assembles to form a perfect unusual dimeric alpha 8 beta 16 barrel. Urate oxidase may be the archetype of an expanding new family of tunnel-shaped proteins that now has three members; tetrahydropterin synthase, GTP cyclohydrolase I and urate oxidase. The structure of the active site of urate oxidase around the 8-azaxanthine inhibitor reveals an original mechanism of oxidation that does not require any ions or prosthetic groups.[1]


  1. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution. Colloc'h, N., el Hajji, M., Bachet, B., L'Hermite, G., Schiltz, M., Prangé, T., Castro, B., Mornon, J.P. Nat. Struct. Biol. (1997) [Pubmed]
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