1eyb
From Proteopedia
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|PDB= 1eyb |SIZE=350|CAPTION= <scene name='initialview01'>1eyb</scene>, resolution 1.9Å | |PDB= 1eyb |SIZE=350|CAPTION= <scene name='initialview01'>1eyb</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ey2|1EY2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyb OCA], [http://www.ebi.ac.uk/pdbsum/1eyb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eyb RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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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| - | ==Disease== | ||
| - | Known disease associated with this structure: Alkaptonuria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607474 607474]] | ||
==About this Structure== | ==About this Structure== | ||
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[[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 Sun Mar 30 20:12:07 2008'' |
Revision as of 17:12, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | Homogentisate 1,2-dioxygenase, with EC number 1.13.11.5 | ||||||
| Related: | 1EY2
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE
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.
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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