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| - | [[Image:1x8j.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1x8j| PDB=1x8j | SCENE= }} | | {{STRUCTURE_1x8j| PDB=1x8j | SCENE= }} |
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| - | '''Crystal structure of retinol dehydratase in complex with androsterone and inactive cofactor PAP'''
| + | ===Crystal structure of retinol dehydratase in complex with androsterone and inactive cofactor PAP=== |
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| - | ==Overview==
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| - | The structure of retinol dehydratase (DHR) from Spodoptera frugiperda, a member of the sulfotransferase superfamily, in complexes with the inactive form of the cofactor PAP 3'-phosphoadenosine 5'-phosphate (PAP) and (1) the product of the reaction with retinol anhydroretinol (AR), (2) the retinoid inhibitor all-trans-4-oxoretinol (OR), and (3) the potent steroid inhibitor androsterone (AND) have been determined and compared to the enzyme complex with PAP and retinol. The structures show that the geometry of the active-site amino acids is largely preserved in the various complexes. However, the beta-ionone rings of the retinoids are oriented differently with respect to side chains that have been shown to be important for the enzymatic reaction. In addition, the DHR:PAP:AND complex reveals a novel mode for steroid binding that contrasts significantly with that for steroid binding in other sulfotransferases. The molecule is displaced and rotated approximately 180 degrees along its length so that there is no acceptor hydroxyl in close proximity to the site of sulfate transfer. This observation explains why steroids are potent inhibitors of retinol dehydratase activity, rather than substrates for sulfonation. Most of the steroid-protein contacts are provided by the alpha-helical cap that distinguishes this member of the superfamily. This observation suggests that in addition to providing a chemical environment that promotes the dehydration of a sulfonated intermediate, the cap may also serve to minimize a promiscuous sulfotransferases activity. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15608121}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15608121 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15608121}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Steroid binding.]] | | [[Category: Steroid binding.]] |
| | [[Category: Sulfotransferase]] | | [[Category: Sulfotransferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:42:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:07:59 2008'' |
Revision as of 07:08, 29 July 2008
Template:STRUCTURE 1x8j
Crystal structure of retinol dehydratase in complex with androsterone and inactive cofactor PAP
Template:ABSTRACT PUBMED 15608121
About this Structure
1X8J is a Single protein structure of sequence from Spodoptera frugiperda. Full crystallographic information is available from OCA.
Reference
The structures of the unique sulfotransferase retinol dehydratase with product and inhibitors provide insight into enzyme mechanism and inhibition., Pakhomova S, Buck J, Newcomer ME, Protein Sci. 2005 Jan;14(1):176-82. Epub 2004 Dec 2. PMID:15608121
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