1s8c

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{{Seed}}
 
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[[Image:1s8c.png|left|200px]]
 
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==Crystal structure of human heme oxygenase in a complex with biliverdine==
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The line below this paragraph, containing "STRUCTURE_1s8c", creates the "Structure Box" on the page.
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<StructureSection load='1s8c' size='340' side='right'caption='[[1s8c]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1s8c]] is a 4 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=1S8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S8C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.19&#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=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene></td></tr>
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{{STRUCTURE_1s8c| PDB=1s8c | SCENE= }}
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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=1s8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s8c OCA], [https://pdbe.org/1s8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s8c RCSB], [https://www.ebi.ac.uk/pdbsum/1s8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s8c ProSAT]</span></td></tr>
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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/s8/1s8c_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=1s8c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heme oxygenase oxidatively cleaves heme to biliverdin, leading to the release of iron and CO through a process in which the heme participates both as a cofactor and as a substrate. Here we report the crystal structure of the product, iron-free biliverdin, in a complex with human HO-1 at 2.19 A. Structural comparisons of the human biliverdin-HO-1 structure with its heme complex and the recently published rat HO-1 structure in a complex with the biliverdin-iron chelate [Sugishima, M., Sakamoto, H., Higashimoto, Y., Noguchi, M., and Fukuyama, K. (2003) J. Biol. Chem. 278, 32352-32358] show two major differences. First, in the absence of an Fe-His bond and solvent structure in the active site, the distal and proximal helices relax and adopt an "open" conformation which most likely encourages biliverdin release. Second, iron-free biliverdin occupies a different position and orientation relative to heme and the biliverdin-iron complex. Biliverdin adopts a more linear conformation and moves from the heme site to an internal cavity. These structural results provide insight into the rate-limiting step in HO-1 catalysis, which is product, biliverdin, release.
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===Crystal structure of human heme oxygenase in a complex with biliverdine===
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Crystal structure of human heme oxygenase-1 in a complex with biliverdin.,Lad L, Friedman J, Li H, Bhaskar B, Ortiz de Montellano PR, Poulos TL Biochemistry. 2004 Apr 6;43(13):3793-801. PMID:15049686<ref>PMID:15049686</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1s8c" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15049686}}, adds the Publication Abstract to the page
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15049686 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15049686}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1S8C 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=1S8C OCA].
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==Reference==
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Crystal structure of human heme oxygenase-1 in a complex with biliverdin., Lad L, Friedman J, Li H, Bhaskar B, Ortiz de Montellano PR, Poulos TL, Biochemistry. 2004 Apr 6;43(13):3793-801. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15049686 15049686]
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[[Category: Heme oxygenase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bhaskar, B.]]
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[[Category: Bhaskar B]]
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[[Category: Friedman, J.]]
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[[Category: Friedman J]]
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[[Category: Lad, L.]]
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[[Category: Lad L]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Montellano, P R.Ortiz de.]]
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[[Category: Ortiz de Montellano PR]]
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[[Category: Poulos, T L.]]
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[[Category: Poulos TL]]
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[[Category: Heme degradation]]
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[[Category: Heme oxygenase-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:46:02 2008''
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Current revision

Crystal structure of human heme oxygenase in a complex with biliverdine

PDB ID 1s8c

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