1ey2
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HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Alkaptonuria OMIM:[607474]
About this StructureAbout this Structure
1EY2 is a Single protein structure of sequence from Homo sapiens with FE2 as ligand. Active as Homogentisate 1,2-dioxygenase, with EC number 1.13.11.5 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human homogentisate dioxygenase., Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE, Nat Struct Biol. 2000 Jul;7(7):542-6. PMID:10876237
Page seeded by OCA on Mon Nov 12 16:47:41 2007