Structure of cytochrome P450eryF involved in erythromycin biosynthesis
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 sever...
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| Veröffentlicht in: | Nature Structural Biology 1995-02, Vol.2 (2), p.144-153 |
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| creator | Cupp-Vickery, Jill R. Poulos, Thomas L. |
| description | 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. |
| doi_str_mv | 10.1038/nsb0295-144 |
| format | Article |
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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. 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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. 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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.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>7749919</pmid><doi>10.1038/nsb0295-144</doi><tpages>10</tpages></addata></record> |
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| language | eng |
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| subjects | Amino Acid Sequence Bacterial Proteins Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Camphor 5-Monooxygenase Catalysis Cytochrome P-450 Enzyme System - chemistry Erythromycin - analogs & derivatives Erythromycin - biosynthesis Erythromycin - metabolism Hydrogen Bonding Hydroxylation Life Sciences Membrane Biology Mixed Function Oxygenases - chemistry Models, Molecular Molecular Sequence Data Oxygen - metabolism Protein Binding Protein Conformation Protein Structure Protein Structure, Secondary Sequence Alignment Sequence Homology, Amino Acid |
| title | Structure of cytochrome P450eryF involved in erythromycin biosynthesis |
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