1EY2

HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)

Summary for 1EY2

• Entry DOI: 10.2210/pdb1ey2/pdb
• Related: 1EYB
• Descriptor: HOMOGENTISATE 1,2-DIOXYGENASE, FE (II) ION (3 entities in total)
• Functional Keywords: jelly roll, beta sandwich, oxidoreductase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 53704.43

Authors

Timm, D.E.,Titus, G.P.,Penalva, M.A.,Mueller, H.A.,de Cordoba, S.M. (deposition date: 2000-05-05, release date: 2000-11-05, Last modification date: 2024-11-20)

Primary citation

Titus, G.P.,Mueller, H.A.,Burgner, J.,Rodriguez De Cordoba, S.,Penalva, M.A.,Timm, D.E.
Crystal structure of human homogentisate dioxygenase.
Nat.Struct.Biol., 7:542-546, 2000

PubMed 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.

PubMed: 10876237
DOI: 10.1038/76756

Experimental method

X-RAY DIFFRACTION (2.3 Å)