Crystallization and X-ray Diffraction Properties of Baeyer-Villiger Monooxygenase MtmOIV from the Mithramycin Biosynthetic Pathway in Streptomyces Argillaceus

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2006 Mar 3

PMID 16511225

Citations 2

Authors

Chenchen Wang

Miranda Gibson

Jurgen Rohr

Marcos A Oliveira

Affiliations

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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.

Citing Articles

Molecular insight into substrate recognition and catalysis of Baeyer-Villiger monooxygenase MtmOIV, the key frame-modifying enzyme in the biosynthesis of anticancer agent mithramycin.

Bosserman M, Downey T, Noinaj N, Buchanan S, Rohr J ACS Chem Biol. 2013; 8(11):2466-77.

PMID: 23992662 PMC: 3830731. DOI: 10.1021/cb400399b.

Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway .

Beam M, Bosserman M, Noinaj N, Wehenkel M, Rohr J Biochemistry. 2009; 48(21):4476-87.

PMID: 19364090 PMC: 2713373. DOI: 10.1021/bi8023509.

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