1eyb

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[[Image:1eyb.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE==
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|PDB= 1eyb |SIZE=350|CAPTION= <scene name='initialview01'>1eyb</scene>, resolution 1.9&Aring;
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<StructureSection load='1eyb' size='340' side='right'caption='[[1eyb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1eyb]] 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=1EYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYB FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyb OCA], [https://pdbe.org/1eyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyb RCSB], [https://www.ebi.ac.uk/pdbsum/1eyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyb ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ey2|1EY2]]
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</table>
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|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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== Disease ==
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}}
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1eyb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eyb ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE'''
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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1EYB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYB OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10876237 10876237]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Homogentisate 1,2-dioxygenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Mueller HA]]
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[[Category: Cordoba, S M.de.]]
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[[Category: Penalva MA]]
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[[Category: Mueller, H A.]]
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[[Category: Timm DE]]
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[[Category: Penalva, M A.]]
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[[Category: Titus GP]]
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[[Category: Timm, D E.]]
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[[Category: De Cordoba SM]]
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[[Category: Titus, G P.]]
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[[Category: beta sandwich]]
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[[Category: jelly roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:12:07 2008''
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Current revision

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

PDB ID 1eyb

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