1EYB: Crystal Structure Of Apo Human Homogentisate Dioxygenase

Citation:
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.
PDB ID: 1EYBDownload
MMDB ID: 14696
PDB Deposition Date: 2000/5/5
Updated in MMDB: 2000/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1EYB: hexameric; determined by author and by software (PISA,PQS)
Molecular Components in 1EYB
Label Count Molecule
Proteins (6 molecules)
6
Homogentisate 1,2-dioxygenase(Gene symbol: HGD)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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