1eyb
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Homogentisate dioxygenase (HGO) cleaves the aromatic ring during the | + | 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== | ==Disease== | ||
| Line 17: | Line 17: | ||
[[Category: Homogentisate 1,2-dioxygenase]] | [[Category: Homogentisate 1,2-dioxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cordoba, S | + | [[Category: Cordoba, S M.de.]] |
| - | [[Category: Mueller, H | + | [[Category: Mueller, H A.]] |
| - | [[Category: Penalva, M | + | [[Category: Penalva, M A.]] |
| - | [[Category: Timm, D | + | [[Category: Timm, D E.]] |
| - | [[Category: Titus, G | + | [[Category: Titus, G P.]] |
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: jelly roll]] | [[Category: jelly roll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:49 2008'' |
Revision as of 10:32, 21 February 2008
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CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE
Contents |
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 Thu Feb 21 12:32:49 2008
