1eyb
From Proteopedia
(New page: 200px<br /> <applet load="1eyb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyb, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1eyb, resolution 1.9Å" /> | caption="1eyb, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE'''<br /> | '''CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Homogentisate_1,2-dioxygenase Homogentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.5 1.13.11.5] Full crystallographic information is available from [http:// | + | 1EYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Homogentisate_1,2-dioxygenase Homogentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.5 1.13.11.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: jelly roll]] | [[Category: jelly roll]] | ||
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Revision as of 13:45, 15 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
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