SOLVING PHASE PROBLEM USING A SE-MET DERIVATIVE OF THE FLAVOENZYME NAD(P)H:ACCEPTOR OXIDOREDUCTASE (FERB)

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Authors	KLUMPLER Tomáš MAREK Jaromír SEDLÁČEK Vojtěch KUČERA Igor
Year of publication	2010
Type	Article in Proceedings
Conference	Materials Structure, vol. 17, no. 1a (2010)
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	phase problem; flavoenzyme; FerB; reductase; crystallography
Description	The flavin adenine dinucleotide-dependent enzyme FerB from Paracoccus denitrificans reduces a range of sub strates, including chromate, ferric complexes, benzoquinones and naphtoquinones. The reduced form of nicotinamide adenine dinucleotide serves as a source of electrons. Recombinant unmodified and selenometionine-substituted (Se-Met) FerB derivatives were crystallized, diffraction data for both forms were collected and the phase problem for Se-Met FerB dimer was solved by three-wavelength multiple anomalous dispersion, followed by the combination of molecular replacement and single-wavelength anomalous diffraction phasing. A molecular replacement solution of unmodified FerB tetramer was obtained using Se-Met structure as a search model.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Molecular basis of cell and tissue regulations Structure, function and regulation of FerB, a broad-specificity bacterial oxidoreductase of a potential ecotechnological relevance Regulation of morphogenesis of plant cells and organs Molecular mechanisms of the cell proliferation and differentiation