1dve

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[[Image:1dve.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME==
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The line below this paragraph, containing "STRUCTURE_1dve", creates the "Structure Box" on the page.
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<StructureSection load='1dve' size='340' side='right'caption='[[1dve]], [[Resolution|resolution]] 2.40&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'>[[1dve]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DVE 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]] 2.4&#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></td></tr>
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{{STRUCTURE_1dve| PDB=1dve | 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=1dve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dve OCA], [https://pdbe.org/1dve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dve RCSB], [https://www.ebi.ac.uk/pdbsum/1dve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dve ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT] 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/dv/1dve_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=1dve ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME'''
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==See Also==
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O(2) and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the delta-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH(-). The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed.
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[[Category: Large Structures]]
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==About this Structure==
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1DVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVE OCA].
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==Reference==
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Crystal structure of rat heme oxygenase-1 in complex with heme., Sugishima M, Omata Y, Kakuta Y, Sakamoto H, Noguchi M, Fukuyama K, FEBS Lett. 2000 Apr 7;471(1):61-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10760513 10760513]
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[[Category: Heme oxygenase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Fukuyama K]]
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[[Category: Fukuyama, K.]]
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[[Category: Kakuta Y]]
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[[Category: Kakuta, Y.]]
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[[Category: Noguchi M]]
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[[Category: Noguchi, M.]]
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[[Category: Omata Y]]
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[[Category: Omata, Y.]]
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[[Category: Sakamoto H]]
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[[Category: Sakamoto, H.]]
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[[Category: Sugishima M]]
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[[Category: Sugishima, M.]]
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[[Category: All alpha]]
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[[Category: Protein-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:19:40 2008''
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Current revision

CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME

PDB ID 1dve

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