A helical lid converts a sulfotransferase to a dehydratase

Nat Struct Biol. 2001 May;8(5):447-51. doi: 10.1038/87617.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution / genetics
  • Animals
  • Benzaldehydes / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Hydro-Lyases / chemistry*
  • Hydro-Lyases / genetics
  • Hydro-Lyases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Structure, Secondary
  • Sequence Alignment
  • Structure-Activity Relationship
  • Sulfates / metabolism
  • Sulfotransferases / chemistry*
  • Sulfotransferases / genetics
  • Sulfotransferases / metabolism*
  • Vitamin A / analogs & derivatives
  • Vitamin A / metabolism
  • Vitamin A / pharmacology

Substances

  • Benzaldehydes
  • Sulfates
  • Vitamin A
  • anhydrovitamin A
  • vanillin
  • Sulfotransferases
  • Hydro-Lyases
  • retinol dehydratase

Associated data

  • PDB/1FMJ
  • PDB/1FML