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Título: | Crystal structure of human homogentisate dioxygenase |
Autor: | Titus, Gregory P.; Mueller, Heather A.; Burgner, John; Rodríguez de Córdoba, Santiago ; Peñalva, Miguel Ángel CSIC ORCID ; Timm, David E. | Fecha de publicación: | jul-2000 | Editor: | Nature Publishing Group | Citación: | Nature Structural Biology 7:542-546 (2000) | Resumen: | Homogentisate dioxygenase (HGO) cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. HGO deficiency causes alkaptonuria (AKU), the first human disease shown to be inherited as a recessive Mendelian trait. Crystal structures of apo-HGO and HGO containing an iron ion have been determined at 1.9 and 2.3 Å resolution, respectively. The HGO protomer, which contains a 280-residue N-terminal domain and a 140-residue C-terminal domain, associates as a hexamer arranged as a dimer of trimers. The active site iron ion is coordinated near the interface between subunits in the HGO trimer by a Glu and two His side chains. HGO represents a new structural class of dioxygenases. The largest group of AKU associated missense mutations affect residues located in regions of contact between subunits | Descripción: | 5 páginas, 4 figuras, 1 tabla -- PAGS nros. 542-546 | Versión del editor: | http://dx.doi.org/10.1038/76756 | URI: | http://hdl.handle.net/10261/71724 | DOI: | 10.1038/76756 | ISSN: | 1072-8368 |
Aparece en las colecciones: | (CIB) Artículos |
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