1eyb

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{{STRUCTURE_1eyb| PDB=1eyb | SCENE= }}
{{STRUCTURE_1eyb| PDB=1eyb | SCENE= }}
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'''CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE'''
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===CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10876237 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10876237}}
==About this Structure==
==About this Structure==
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[[Category: Beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:40:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:12:24 2008''

Revision as of 23:12, 30 June 2008

Image:1eyb.png

Template:STRUCTURE 1eyb

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Template:ABSTRACT PUBMED 10876237

About this Structure

1EYB is a Single protein structure of sequence from Homo sapiens. 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

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