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Papers In Press, published online ahead of print August 30, 2002
Physikalische Biochemie, Max-Planck-Institut für molekulare Physiologie, Dortmund D-44227
Corresponding Author: ilme.schlichting{at}mpi-dortmund.mpg.de
Gene-inactivation studies point to the involvement of OxyB in catalyzing the first oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. The oxyB gene has been cloned and sequenced from the vancomycin producer Amycolatopsis orientalis, and the hemoprotein has been produced in Escherichia coli, crystallized and its structure determined to 1.7Å resolution. OxyB gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite or by spinach ferredoxin and ferredoxin reductase, the CO-ligated form gave a 450 nm peak in a UV-difference spectrum. Addition of putative heptapeptide substrates to resting OxyB produced type-I changes to the UV spectrum, but no turnover was observed in the presence of ferredoxin and ferredoxin reductase, showing that either the peptides or the reduction system, or both, are insufficient to support a full catalytic cycle. OxyB exhibits the typical P450-fold, with helix L containing the signature sequence FGHGXHXCLG and Cys347 being the proximal axial thiolate ligand of the heme iron. The structural similarity of OxyB is highest to P450nor, P450terp, CYP119, and P450eryF. In OxyB, the F and G helices are rotated out of the active site compared to P450nor, resulting in a much more open active site, consistent with the larger size of the substrate, possibly a heptapeptide conjugated to a carrier protein.
J. Biol. Chem, 10.1074/jbc.M206342200
Submitted on June 26, 2002
Revised on August 29, 2002
Accepted on August 30, 2002
Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis
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