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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Chenchen WangMarcos A Oliveira

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.

References

Aug 22, 2001·Protein Science : a Publication of the Protein Society·O Dym, D Eisenberg
Jul 3, 2003·Trends in Biotechnology·Veronique AlphandJohn M Woodley
Nov 6, 2003·Organic & Biomolecular Chemistry·María C GutiérrezRoland Furstoss
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Aug 26, 2004·Proceedings of the National Academy of Sciences of the United States of America·Enrico MalitoAndrea Mattevi

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Citations

Oct 3, 2006·Applied Microbiology and Biotechnology·Felipe LombóCarmen Méndez
May 23, 2006·Journal of Biotechnology·W J H van BerkelM W Fraaije

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