Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus.
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.
Wang
Chenchen
C
Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536-0082, USA.
Gibson
Miranda
M
Rohr
Jurgen
J
Oliveira
Marcos A
MA
D003460:Crystallization; D019281:Dimerization; D019384:Nucleic Acid Synthesis Inhibitors / Q000737:chemistry / Q000378:metabolism; D017785:Photons; D008926:Plicamycin / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012645:Selenomethionine / Q000737:chemistry; D013302:Streptomyces / Q000201:enzymology*; D017356:Synchrotrons; D014961:X-Ray Diffraction
D019384:Nucleic Acid Synthesis Inhibitors; D012645:Selenomethionine; D008926:Plicamycin