5YSW
Crystal Structure Analysis of Rif16 in complex with R-L
Summary for 5YSW
| Entry DOI | 10.2210/pdb5ysw/pdb |
| Descriptor | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, (2S,12E,14E,16S,17S,18R,19R,20R,21S,22R,23S,24E)-21-(acetyloxy)-5,6,17,19-tetrahydroxy-23-methoxy-2,4,12,16,18,20,22-heptamethyl-1,11-dioxo-1,2-dihydro-2,7-(epoxypentadeca[1,11,13]trienoimino)naphtho[2,1-b]furan-9-yl hydroxyacetate, ... (4 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 | 50157.68 |
| Authors | Li, F.W.,Qi, F.F.,Xiao, Y.L.,Zhao, G.P.,Li, S.Y. (deposition date: 2017-11-15, release date: 2018-07-04, Last modification date: 2023-11-22) |
| 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 (2.6 Å) |
Structure validation
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