The structure of a retinal-forming carotenoid oxygenase

Science. 2005 Apr 8;308(5719):267-9. doi: 10.1126/science.1108965.


Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Escherichia coli
  • Humans
  • Molecular Sequence Data
  • Oxygenases / chemistry*
  • Protein Conformation
  • Recombinant Proteins
  • Retinaldehyde / chemistry*
  • Synechocystis / enzymology*
  • Synechocystis / genetics


  • Recombinant Proteins
  • Oxygenases
  • Retinaldehyde

Associated data

  • PDB/2BIW