1EYB
CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE
Summary for 1EYB
| Entry DOI | 10.2210/pdb1eyb/pdb |
| Related | 1EY2 |
| Descriptor | HOMOGENTISATE 1,2-DIOXYGENASE (2 entities in total) |
| Functional Keywords | jelly roll, beta sandwich, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 53648.58 |
| 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: 2021-11-03) |
| 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 Cited by 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: 10876237DOI: 10.1038/76756 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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