A helical lid converts a sulfotransferase to a dehydratase

We report here the crystal structure of retinol dehydratase, an enzyme that catalyzes the synthesis of anhydroretinol. The enzyme is a member of the sulfotransferase superfamily and its crystal structure reveals the insertion of a helical lid into a canonical sulfotransferase fold. Site-directed mut...

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Veröffentlicht in:Nature Structural Biology 2001-05, Vol.8 (5), p.447-451
Hauptverfasser: Pakhomova, Svetlana, Kobayashi, Mime, Buck, Jochen, Newcomer, Marcia E.
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Sprache:eng
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Zusammenfassung:We report here the crystal structure of retinol dehydratase, an enzyme that catalyzes the synthesis of anhydroretinol. The enzyme is a member of the sulfotransferase superfamily and its crystal structure reveals the insertion of a helical lid into a canonical sulfotransferase fold. Site-directed mutations demonstrate that this inserted lid is necessary for anhydroretinol production but not for sulfonation; thus, insertion of a helical lid can convert a sulfotransferase into a dehydratase.
ISSN:1072-8368
1545-9993
1545-9985
DOI:10.1038/87617