2q32

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[[Image:2q32.jpg|left|200px]]
[[Image:2q32.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2q32 |SIZE=350|CAPTION= <scene name='initialview01'>2q32</scene>, resolution 2.400&Aring;
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The line below this paragraph, containing "STRUCTURE_2q32", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Oxn+Binding+Site+For+Residue+A+301'>AC1</scene> and <scene name='pdbsite=AC2:Oxn+Binding+Site+For+Residue+B+301'>AC2</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=OXN:OXTOXYNOL-10'>OXN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= Hs.284279, HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00232 HemeO]</span>
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{{STRUCTURE_2q32| PDB=2q32 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q32 OCA], [http://www.ebi.ac.uk/pdbsum/2q32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q32 RCSB]</span>
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}}
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'''Crystal structure of human heme oxygenase-2 C127A (HO-2)'''
'''Crystal structure of human heme oxygenase-2 C127A (HO-2)'''
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[[Category: Jr., G N.Phillips.]]
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[[Category: center for eukaryotic structural genomic]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: cesg]]
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[[Category: Cesg]]
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[[Category: heme oxygenase]]
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[[Category: Heme oxygenase]]
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[[Category: ho-2]]
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[[Category: Ho-2]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: psi]]
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[[Category: Psi]]
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[[Category: Structural genomics medical relevance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:14:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:43:56 2008''
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Revision as of 11:14, 4 May 2008

Image:2q32.jpg

Template:STRUCTURE 2q32

Crystal structure of human heme oxygenase-2 C127A (HO-2)


Overview

Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.

About this Structure

2Q32 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:17965015 Page seeded by OCA on Sun May 4 14:14:05 2008

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