1eyb

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spinqualitylabelsall models 1eyb, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Alkaptonuria OMIM:[607474]

About this Structure

1EYB is a Single protein structure of sequence from Homo sapiens. Active as Homogentisate 1,2-dioxygenase, with EC number 1.13.11.5 Full crystallographic information is available from OCA.

Reference

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 Fri Feb 15 15:45:13 2008