We report here the crystal structure of retinol dehydratase, an enzyme that
catalyzes the synthesis of anhydroretinol. The enzyme is a member of the s
ulfotransferase superfamily and its crystal structure reveals the insertion
of a helical lid into a canonical sulfotransferase fold. Site-directed mut
ations demonstrate that this inserted lid is necessary for anhydroretinol p
roduction but not for sulfonation; thus, insertion of a helical lid can con
vert a sulfotransferase into a dehydratase.