1dve
From Proteopedia
(New page: 200px<br /><applet load="1dve" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dve, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1dve.gif|left|200px]]<br /><applet load="1dve" size=" | + | [[Image:1dve.gif|left|200px]]<br /><applet load="1dve" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dve, resolution 2.40Å" /> | caption="1dve, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME'''<br /> | '''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heme oxygenase catalyzes the oxidative cleavage of protoheme to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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:// | + | 1DVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-substrate complex]] | [[Category: protein-substrate complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:59 2008'' |
Revision as of 10:20, 21 February 2008
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CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME
Overview
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.
About this Structure
1DVE is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Heme oxygenase, with EC number 1.14.99.3 Full crystallographic information is available from OCA.
Reference
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:10760513
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