1eyb

From Proteopedia

(Difference between revisions)

Revision as of 16:23, 29 September 2014

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Structural highlights

1eyb is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1ey2
Activity:	Homogentisate 1,2-dioxygenase, with EC number 1.13.11.5
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[HGD_HUMAN] Defects in HGD are the cause of alkaptonuria (AKU) [MIM: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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Function

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fernandez-Canon JM, Granadino B, Beltran-Valero de Bernabe D, Renedo M, Fernandez-Ruiz E, Penalva MA, Rodriguez de Cordoba S. The molecular basis of alkaptonuria. Nat Genet. 1996 Sep;14(1):19-24. PMID:8782815 doi:10.1038/ng0996-19
↑ Gehrig A, Schmidt SR, Muller CR, Srsen S, Srsnova K, Kress W. Molecular defects in alkaptonuria. Cytogenet Cell Genet. 1997;76(1-2):14-6. PMID:9154114
↑ Beltran-Valero de Bernabe D, Granadino B, Chiarelli I, Porfirio B, Mayatepek E, Aquaron R, Moore MM, Festen JJ, Sanmarti R, Penalva MA, de Cordoba SR. Mutation and polymorphism analysis of the human homogentisate 1, 2-dioxygenase gene in alkaptonuria patients. Am J Hum Genet. 1998 Apr;62(4):776-84. PMID:9529363
↑ Higashino K, Liu W, Ohkawa T, Yamamoto T, Fukui K, Ohno M, Imanishi H, Iwasaki A, Amuro Y, Hada T. A novel point mutation associated with alkaptonuria. Clin Genet. 1998 Mar;53(3):228-9. PMID:9630082
↑ Beltran-Valero de Bernabe D, Jimenez FJ, Aquaron R, Rodriguez de Cordoba S. Analysis of alkaptonuria (AKU) mutations and polymorphisms reveals that the CCC sequence motif is a mutational hot spot in the homogentisate 1,2 dioxygenase gene (HGO). Am J Hum Genet. 1999 May;64(5):1316-22. PMID:10205262 doi:S0002-9297(07)62276-9
↑ Felbor U, Mutsch Y, Grehn F, Muller CR, Kress W. Ocular ochronosis in alkaptonuria patients carrying mutations in the homogentisate 1,2-dioxygenase gene. Br J Ophthalmol. 1999 Jun;83(6):680-3. PMID:10340975
↑ Muller CR, Fregin A, Srsen S, Srsnova K, Halliger-Keller B, Felbor U, Seemanova E, Kress W. Allelic heterogeneity of alkaptonuria in Central Europe. Eur J Hum Genet. 1999 Sep;7(6):645-51. PMID:10482952 doi:10.1038/sj.ejhg.5200343
↑ Beltran-Valero de Bernabe D, Peterson P, Luopajarvi K, Matintalo P, Alho A, Konttinen Y, Krohn K, Rodriguez de Cordoba S, Ranki A. Mutational analysis of the HGO gene in Finnish alkaptonuria patients. J Med Genet. 1999 Dec;36(12):922-3. PMID:10594001
↑ Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE. Crystal structure of human homogentisate dioxygenase. Nat Struct Biol. 2000 Jul;7(7):542-6. PMID:10876237 doi:http://dx.doi.org/10.1038/76756

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eyb"

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1eyb|  PDB=1eyb  |  SCENE=  }}
+==CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE==
-===CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE===
+<StructureSection load='1eyb' size='340' side='right' caption='[[1eyb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-{{ABSTRACT_PUBMED_10876237}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1eyb]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EYB FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ey2|1ey2]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1eyb RCSB], [http://www.ebi.ac.uk/pdbsum/1eyb PDBsum]</span></td></tr>
+<table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN]] Defects in HGD are the cause of alkaptonuria (AKU) [MIM:[http://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 ==
-==Disease==
+== Evolutionary Conservation ==
-[[http://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN]] Defects in HGD are the cause of alkaptonuria (AKU) [MIM:[http://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>
+[[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/1eyb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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.
-==About this Structure==
+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>
-[[1eyb]] is a 1 chain structure with 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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:010876237</ref><references group="xtra"/><references/>
+</div>
+==See Also==
+*[[Dioxygenase|Dioxygenase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
 [[Category: Homogentisate 1,2-dioxygenase]]

1eyb

From Proteopedia

Revision as of 16:23, 29 September 2014

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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