1ey2
From Proteopedia
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| - | {{STRUCTURE_1ey2| PDB=1ey2 | SCENE= }} | ||
| - | ===HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)=== | ||
| - | {{ABSTRACT_PUBMED_10876237}} | ||
| - | == | + | ==HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)== |
| - | [[http://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN | + | <StructureSection load='1ey2' size='340' side='right'caption='[[1ey2]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ey2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EY2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ey2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ey2 OCA], [https://pdbe.org/1ey2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ey2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ey2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ey2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN] Defects in HGD are the cause of alkaptonuria (AKU) [MIM:[https://omim.org/entry/203500 203500]. AKU is an autosomal recessive error of metabolism characterized by an increase in the level of homogentisic acid. The clinical manifestations of AKU are urine that turns dark on standing and alkalinization, black ochronotic pigmentation of cartilage and collagenous tissues, and spine arthritis.<ref>PMID:8782815</ref> <ref>PMID:9154114</ref> <ref>PMID:9529363</ref> <ref>PMID:9630082</ref> <ref>PMID:10205262</ref> <ref>PMID:10340975</ref> <ref>PMID:10482952</ref> <ref>PMID:10594001</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1ey2_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ey2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:10876237</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 1ey2" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Mueller HA]] | |
| - | [[Category: Mueller | + | [[Category: Penalva MA]] |
| - | [[Category: Penalva | + | [[Category: Timm DE]] |
| - | [[Category: Timm | + | [[Category: Titus GP]] |
| - | [[Category: Titus | + | [[Category: De Cordoba SM]] |
| - | [[Category: | + | |
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Current revision
HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)
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