1xk0

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{{STRUCTURE_1xk0| PDB=1xk0 | SCENE= }}
 
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===Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1===
 
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{{ABSTRACT_PUBMED_15690204}}
 
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==Disease==
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==Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1==
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[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
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<StructureSection load='1xk0' size='340' side='right'caption='[[1xk0]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[1xk0]] is a 2 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=1XK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XK0 FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
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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]] 2.18&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></td></tr>
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==About this Structure==
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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=1xk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xk0 OCA], [https://pdbe.org/1xk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xk0 RCSB], [https://www.ebi.ac.uk/pdbsum/1xk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xk0 ProSAT]</span></td></tr>
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[[1xk0]] is a 2 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=1XK0 OCA].
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[https://omim.org/entry/614034 614034]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
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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/xk/1xk0_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=1xk0 ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Heme oxygenase|Heme oxygenase]]
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015690204</ref><references group="xtra"/><references/>
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__TOC__
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[[Category: Heme oxygenase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Koshkin, A.]]
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[[Category: Large Structures]]
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[[Category: Lad, L.]]
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[[Category: Koshkin A]]
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[[Category: Montellano, P R.Ortiz de.]]
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[[Category: Lad L]]
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[[Category: Poulos, T L.]]
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[[Category: Ortiz de Montellano PR]]
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[[Category: Heme]]
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[[Category: Poulos TL]]
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[[Category: Heme degredation]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1

PDB ID 1xk0

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