1fml | pdb_00001fml

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CRYSTAL STRUCTURE OF RETINOL DEHYDRATASE IN A COMPLEX WITH RETINOL AND PAP

File:1fml.gif


1fml, resolution 2.75Å

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Overview

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.

About this Structure

1FML is a Single protein structure of sequence from Spodoptera frugiperda with CA, A3P and RTL as ligands. Full crystallographic information is available from OCA.

Reference

A helical lid converts a sulfotransferase to a dehydratase., Pakhomova S, Kobayashi M, Buck J, Newcomer ME, Nat Struct Biol. 2001 May;8(5):447-51. PMID:11323722

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