5YSM
Crystal Structure Analysis of Rif16
Summary for 5YSM
| Entry DOI | 10.2210/pdb5ysm/pdb |
| Descriptor | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450, rifamycin, metal binding protein, oxidoreductase |
| Biological source | Amycolatopsis mediterranei (strain U-32) |
| Total number of polymer chains | 1 |
| Total formula weight | 49401.87 |
| Authors | Li, F.W.,Qi, F.F.,Xiao, Y.L.,Zhao, G.P.,Li, S.Y. (deposition date: 2017-11-14, release date: 2018-07-04, Last modification date: 2024-03-27) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
