2rgz
From Proteopedia
(New page: 200px<br /> <applet load="2rgz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rgz, resolution 2.610Å" /> '''Ensemble refinemen...) |
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| - | [[Image:2rgz. | + | [[Image:2rgz.jpg|left|200px]]<br /><applet load="2rgz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2rgz" size=" | + | |
caption="2rgz, resolution 2.610Å" /> | caption="2rgz, resolution 2.610Å" /> | ||
'''Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme'''<br /> | '''Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 2RGZ 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 HEM 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] Full crystallographic information is available from [http:// | + | 2RGZ 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 265'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGZ OCA]. |
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| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17965015 17965015] | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: structural genomics medical relevance]] | [[Category: structural genomics medical relevance]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:44:44 2008'' |
Revision as of 08:44, 23 January 2008
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Ensemble refinement of the protein 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
2RGZ 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 Wed Jan 23 10:44:44 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 | Ensemble refinement | Ho-2 | Iron | Metal-binding | Microsome | Oxidoreductase | Polymorphism | Protein structure initiative | Psi | Refinement methodology development | Structural genomics | Structural genomics community request | Structural genomics medical relevance
