1dve

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[[Image:1dve.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1dve| PDB=1dve | SCENE= }}
{{STRUCTURE_1dve| PDB=1dve | SCENE= }}
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'''CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME'''
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===CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10760513 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10760513}}
==About this Structure==
==About this Structure==
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[[Category: All alpha]]
[[Category: All alpha]]
[[Category: Protein-substrate complex]]
[[Category: Protein-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:19:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:40:36 2008''

Revision as of 20:40, 30 June 2008

Image:1dve.png

Template:STRUCTURE 1dve

CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME

Template:ABSTRACT PUBMED 10760513

About this Structure

1DVE is a Single protein structure of sequence from Rattus norvegicus. 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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