1dve: Difference between revisions
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[[Image:1dve.gif|left|200px]] | [[Image:1dve.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME''' | {{Structure | ||
|PDB= 1dve |SIZE=350|CAPTION= <scene name='initialview01'>1dve</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DVE is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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] | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: protein-substrate complex]] | [[Category: protein-substrate complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:58 2008'' | ||
Revision as of 11:45, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Activity: | Heme oxygenase, with EC number 1.14.99.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME
OverviewOverview
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 StructureAbout this Structure
1DVE is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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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