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| - | [[Image:2iag.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2iag| PDB=2iag | SCENE= }} | | {{STRUCTURE_2iag| PDB=2iag | SCENE= }} |
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| - | '''Crystal structure of human prostacyclin synthase'''
| + | ===Crystal structure of human prostacyclin synthase=== |
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| - | ==Overview==
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| - | Prostacyclin synthase (PGIS) catalyzes an isomerization of prostaglandin H(2) to prostacyclin, a potent mediator of vasodilation and anti-platelet aggregation. Here, we report the crystal structure of human PGIS at 2.15 A resolution, which represents the first three-dimensional structure of a class III cytochrome P450. While notable sequence divergence has been recognized between PGIS and other P450s, PGIS exhibits the typical triangular prism-shaped P450 fold with only moderate structural differences. The conserved acid-alcohol pair in the I helix of P450s is replaced by residues G286 and N287 in PGIS, but the distinctive disruption of the I helix and the presence of a nearby water channel remain conserved. The side-chain of N287 appears to be positioned to facilitate the endoperoxide bond cleavage, suggesting a functional conservation of this residue in O-O bond cleavage. A combination of bent I helix and tilted B' helix creates a channel extending from the heme distal pocket, which seemingly allows binding of various ligands; however, residue W282, placed in this channel at a distance of 8.4 A from the iron with its indole side-chain lying parallel with the porphyrin plane, may serve as a threshold to exclude most ligands from binding. Additionally, a long "meander" region protruding from the protein surface may impede electron transfer. Although the primary sequence of the PGIS cysteine ligand loop diverges significantly from the consensus, conserved tertiary structure and hydrogen bonding pattern are observed for this region. The substrate-binding model was constructed and the structural basis for prostacyclin biosynthesis is discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17020766}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17020766 is the PubMed ID number. |
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| | ==Disease== | | ==Disease== |
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| | [[Category: Hemoprotein]] | | [[Category: Hemoprotein]] |
| | [[Category: Prostacyclin synthase]] | | [[Category: Prostacyclin synthase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:15:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:13:27 2008'' |
Revision as of 00:13, 29 July 2008
Template:STRUCTURE 2iag
Crystal structure of human prostacyclin synthase
Template:ABSTRACT PUBMED 17020766
Disease
Known disease associated with this structure: Hypertension, essential OMIM:[601699]
About this Structure
2IAG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human prostacyclin synthase., Chiang CW, Yeh HC, Wang LH, Chan NL, J Mol Biol. 2006 Dec 1;364(3):266-74. Epub 2006 Sep 20. PMID:17020766
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