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Structure of cytochrome P450eryF involved in erythromycin biosynthesis

Nature Structural Biology volume 2, pages 144–153 (1995)Cite this article

Abstract

Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several α-helices. The largest difference occurs in the B′ helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction.

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, and Department of Physiology and Biophysics, University of California, Irvine, California, 92717, USA

    Jill R. Cupp-Vickery & Thomas L. Poulos

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  1. Jill R. Cupp-Vickery
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  2. Thomas L. Poulos
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Cupp-Vickery, J., Poulos, T. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat Struct Mol Biol 2, 144–153 (1995). https://doi.org/10.1038/nsb0295-144

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