title: Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
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 alpha-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.
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine 92717, USA.
authors.forename: J R
authors.initials: JR
authors.lastname: Cupp-Vickery
authors.forename: T L
authors.initials: TL
authors.lastname: Poulos
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D004917:Erythromycin / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000378:metabolism; D006860:Hydrogen Bonding; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010100:Oxygen / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; C034277:6-deoxyerythronolide B; D004917:Erythromycin; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C054444:eryF protein, Saccharopolyspora erythraea; D019475:Camphor 5-Monooxygenase; D010100:Oxygen