Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Nov 1;61(Pt 11):1023-6. doi: 10.1107/S1744309105033221. Epub 2005 Oct 28.

Abstract

The Baeyer-Villiger monooxygenase MtmOIV from Streptomyces argillaceus is a 56 kDa FAD-dependent and NADPH-dependent enzyme that is responsible for the key frame-modifying step in the biosynthesis of the natural product mithramycin. Crystals of MtmOIV were flash-cooled and diffracted to 2.69 A resolution using synchrotron radiation on beamline SER-CAT 22-ID at the Advanced Photon Source. Crystals of MtmOIV are monoclinic and light-scattering data reveal that the enzyme forms dimers in solution. The rotation function suggests the presence of two dimers in the asymmetric unit. L-Selenomethionine-incorporated MtmOIV has been obtained. Structural solution combining molecular-replacement phases and anomalous phases from selenium is in progress.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Dimerization
  • Nucleic Acid Synthesis Inhibitors / chemistry
  • Nucleic Acid Synthesis Inhibitors / metabolism
  • Photons
  • Plicamycin / chemistry
  • Plicamycin / metabolism*
  • Protein Conformation
  • Selenomethionine / chemistry
  • Streptomyces / enzymology*
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Nucleic Acid Synthesis Inhibitors
  • Selenomethionine
  • Plicamycin