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Papers In Press, published online ahead of print July 29, 2003
J. Biol. Chem, 10.1074/jbc.M306486200
Submitted on June 18, 2003
Revised on July 25, 2003
Accepted on July 29, 2003

Crystal structure of oxyC a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis

Olena Pylypenko, Francesca Vitali, Katja Zerbe, John A. Robinson, and Ilme Schlichting

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 OxyC in catalyzing the last oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. Presently, the substrate and exact timing of the OxyC reaction is unknown. The substrate might be the bicyclic heptapeptide or a thioester derivative bound to a protein carrier domain. OxyC from the vancomycin producer Amycolatopsis orientalis was produced in Escherichia coli, crystallized and its structure determined to 1.9 Å resolution. OxyC gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite the CO- ligated form gave a 450 nm peak in a UV-difference spectrum. Addition of vancomycin aglycon to OxyC produced type-I changes to the UV spectrum. OxyC exhibits the typical P450-fold, with the Cys-ligand loop containing the signature sequence FGHGXHXCLG and Cys356 being the proximal axial thiolate ligand of the heme iron. The observation of a water molecule bound to the heme iron is consistent with the UV-Vis spectra of OxyC indicating a low spin heme. A polyethylene glycol molecule occupying the active site might mimic the bicyclic heptapeptide substrate. Analysis of the structures of Oxy proteins and other P450s indicates regions that might be involved in binding of the redox partner and possibly the protein carrier domain.


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