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- Title
Crystal structure of human homogentisate dioxygenase.
- Authors
Titus, G P; Mueller, H A; Burgner, J; Rodríguez De Córdoba, S; Peñalva, M A; Timm, D E
- Abstract
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 A 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.
- Publication
Nature structural biology, 2000, Vol 7, Issue 7, p542
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/76756