1ey2: Difference between revisions
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|PDB= 1ey2 |SIZE=350|CAPTION= <scene name='initialview01'>1ey2</scene>, resolution 2.3Å | |PDB= 1ey2 |SIZE=350|CAPTION= <scene name='initialview01'>1ey2</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <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=[[1eyb|1EYB]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ey2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ey2 OCA], [http://www.ebi.ac.uk/pdbsum/1ey2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ey2 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Timm, D E.]] | [[Category: Timm, D E.]] | ||
[[Category: Titus, G P.]] | [[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 Sun Mar 30 20:11:55 2008'' | ||
