5YSM
Crystal Structure Analysis of Rif16
5YSM の概要
| エントリーDOI | 10.2210/pdb5ysm/pdb |
| 分子名称 | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| 機能のキーワード | cytochrome p450, rifamycin, metal binding protein, oxidoreductase |
| 由来する生物種 | Amycolatopsis mediterranei (strain U-32) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 49401.87 |
| 構造登録者 | Li, F.W.,Qi, F.F.,Xiao, Y.L.,Zhao, G.P.,Li, S.Y. (登録日: 2017-11-14, 公開日: 2018-07-04, 最終更新日: 2024-03-27) |
| 主引用文献 | Qi, F.,Lei, C.,Li, F.,Zhang, X.,Wang, J.,Zhang, W.,Fan, Z.,Li, W.,Tang, G.L.,Xiao, Y.,Zhao, G.,Li, S. Deciphering the late steps of rifamycin biosynthesis. Nat Commun, 9:2342-2342, 2018 Cited by PubMed Abstract: Rifamycin-derived drugs, including rifampin, rifabutin, rifapentine, and rifaximin, have long been used as first-line therapies for the treatment of tuberculosis and other deadly infections. However, the late steps leading to the biosynthesis of the industrially important rifamycin SV and B remain largely unknown. Here, we characterize a network of reactions underlying the biosynthesis of rifamycin SV, S, L, O, and B. The two-subunit transketolase Rif15 and the cytochrome P450 enzyme Rif16 are found to mediate, respectively, a unique C-O bond formation in rifamycin L and an atypical P450 ester-to-ether transformation from rifamycin L to B. Both reactions showcase interesting chemistries for these two widespread and well-studied enzyme families. PubMed: 29904078DOI: 10.1038/s41467-018-04772-x 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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