1we1

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{{STRUCTURE_1we1| PDB=1we1 | SCENE= }}
{{STRUCTURE_1we1| PDB=1we1 | SCENE= }}
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'''Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme'''
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===Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme===
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==Overview==
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Heme oxygenase (HO) catalyzes the oxidative degradation of heme utilizing molecular oxygen and reducing equivalents. In photosynthetic organisms, HO functions in the biosynthesis of such open-chain tetrapyrroles as phyto-chromobilin and phycobilins, which are involved in the signal transduction for light responses and light harvesting for photosynthesis, respectively. We have determined the first crystal structure of a HO-1 from a photosynthetic organism, Synechocystis sp. PCC 6803 (Syn HO-1), in complex with heme at 2.5 A resolution. Heme-Syn HO-1 shares a common folding with other heme-HOs. Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity. In addition, 2-propanol derived from the crystallization solution occupied the hydrophobic cavity, which is proposed to be a CO trapping site in rat HO-1 that suppresses product inhibition. Although Syn HO-1 and mammalian HO-1 are similar in overall structure and amino acid sequence (57% similarity vs. human HO-1), their molecular surfaces differ in charge distribution. The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1. This feature is suited to the selective binding of ferredoxin, the physiological redox partner of Syn HO-1; the molecular size of ferredoxin is approximately 10 kDa whereas the size of NADPH-cytochrome P450 reductase, a reducing partner of mammalian HO-1, is approximately 77 kDa. A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.
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The line below this paragraph, {{ABSTRACT_PUBMED_15560792}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15560792 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15560792}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme., Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K, Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15560792 15560792]
Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme., Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K, Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15560792 15560792]
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Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis. Properties of the heme complex of recombinant active enzyme., Migita CT, Zhang X, Yoshida T, Eur J Biochem. 2003 Feb;270(4):687-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12581208 12581208]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:31:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:08:39 2008''

Revision as of 14:08, 28 July 2008

Image:1we1.png

Template:STRUCTURE 1we1

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme

Template:ABSTRACT PUBMED 15560792

About this Structure

1WE1 is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme., Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K, Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:15560792

Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis. Properties of the heme complex of recombinant active enzyme., Migita CT, Zhang X, Yoshida T, Eur J Biochem. 2003 Feb;270(4):687-98. PMID:12581208

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