2qpp
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Heme oxygenase (HO) catalyzes the first step in the heme degradation | + | 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== | ==About this Structure== | ||
| - | 2QPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Hem Binding Site For Residue A 300'>AC1</scene> and <scene name='pdbsite=AC2:Hem Binding Site For Residue B 300'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPP OCA]. | + | 2QPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Hem+Binding+Site+For+Residue+A+300'>AC1</scene> and <scene name='pdbsite=AC2:Hem+Binding+Site+For+Residue+B+300'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPP OCA]. |
==Reference== | ==Reference== | ||
| - | Comparison of | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17965015 17965015] |
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bianchetti, C | + | [[Category: Bianchetti, C M.]] |
| - | [[Category: Bingman, C | + | [[Category: Bingman, C A.]] |
[[Category: Bitto, E.]] | [[Category: Bitto, E.]] | ||
| - | [[Category: CESG, Center | + | [[Category: CESG, Center for Eukaryotic Structural Genomics.]] |
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
| - | [[Category: Wesenberg, G | + | [[Category: Wesenberg, G E.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: center for eukaryotic structural genomics]] | [[Category: center for eukaryotic structural genomics]] | ||
| Line 36: | Line 36: | ||
[[Category: structural genomics medical relevance]] | [[Category: structural genomics medical relevance]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:11 2008'' |
Revision as of 16:41, 21 February 2008
|
Crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme
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
2QPP is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Heme oxygenase, with EC number 1.14.99.3 Known structural/functional Sites: and . 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 Thu Feb 21 18:41:11 2008
Categories: Heme oxygenase | Homo sapiens | Single protein | Bianchetti, C M. | Bingman, C A. | Bitto, E. | CESG, Center for Eukaryotic Structural Genomics. | Jr., G N.Phillips. | Wesenberg, G E. | HEM | Center for eukaryotic structural genomics | Cesg | Endoplasmic reticulum | Ho-2 | Iron | Metal-binding | Microsome | Oxidoreductase | Polymorphism | Protein structure initiative | Psi | Structural genomics community request | Structural genomics medical relevance
