NDLI: The structures of the unique sulfotransferase retinol dehydratase with product and inhibitors provide insight into enzyme mechanism and inhibition.

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The structures of the unique sulfotransferase retinol dehydratase with product and inhibitors provide insight into enzyme mechanism and inhibition.

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The structures of the unique sulfotransferase retinol dehydratase with product and inhibitors provide insight into enzyme mechanism and inhibition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Buck, Jochen Newcomer, Marcia E. Pakhomova, Svetlana
Description	Country affiliation: United States Author Affiliation: Pakhomova S ( Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.)
Abstract	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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hydro-lyases Antagonists & Inhibitors Chemistry Spodoptera Enzymology Sulfotransferases Classification Vitamin A Analogs & Derivatives Amino Acid Sequence Androsterone Pharmacology Animals Anopheles Gambiae Binding Sites Catalysis Crystallography, X-ray Drosophila Melanogaster Macromolecular Substances Mice Molecular Sequence Data Molecular Structure Protein Structure, Secondary Sequence Alignment Sequence Homology, Amino Acid Structure-activity Relationship Substrate Specificity Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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