Crystallization and preliminary X-ray diffraction studies of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of the polyketide actinorhodin

Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):481-3. doi: 10.1107/s0907444900001189.

Abstract

The aromatic monooxygenase ActVA-Orf6 from Streptomyces coelicolor A3(2) that catalyses an unusual oxidation on the actinorhodin biosynthetic pathway has been crystallized. The crystals diffract to 1.73 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.95, b = 59.29, c = 71.67 A. Solvent-content (44%) and self-rotation function calculations predict the presence of two molecules in the asymmetric unit. Structure determination should provide further insight into the enzyme mechanism and aid in the design of biosynthetic pathways to produce new polyketide natural products with novel functionality.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anthraquinones / metabolism
  • Anti-Bacterial Agents / biosynthesis
  • Crystallization
  • Crystallography, X-Ray
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / isolation & purification
  • Mixed Function Oxygenases / metabolism
  • Streptomyces / enzymology*

Substances

  • Anthraquinones
  • Anti-Bacterial Agents
  • Mixed Function Oxygenases
  • actinorhodin