3W8X
The complex structure of EncM with trifluorotriketide
Summary for 3W8X
| Entry DOI | 10.2210/pdb3w8x/pdb |
| Related | 3W8W 3W8Y 3W8Z |
| Descriptor | Putative FAD-dependent oxygenase EncM, FLAVIN-ADENINE DINUCLEOTIDE, 6,6,6-trifluoro-1-phenylhexane-1,3,5-trione, ... (5 entities in total) |
| Functional Keywords | monooxygenase, flavin binding, oxidoreductase |
| Biological source | Streptomyces maritimus |
| Total number of polymer chains | 2 |
| Total formula weight | 103006.99 |
| Authors | Teufel, R.,Miyanaga, A.,Stull, F.,Michaudel, Q.,Louie, G.,Noel, J.P.,Baran, P.S.,Palfey, B.,Moore, B.S. (deposition date: 2013-03-22, release date: 2013-10-30, Last modification date: 2023-11-08) |
| Primary citation | Teufel, R.,Miyanaga, A.,Michaudel, Q.,Stull, F.,Louie, G.,Noel, J.P.,Baran, P.S.,Palfey, B.,Moore, B.S. Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature, 503:552-556, 2013 Cited by PubMed Abstract: Flavoproteins catalyse a diversity of fundamental redox reactions and are one of the most studied enzyme families. As monooxygenases, they are universally thought to control oxygenation by means of a peroxyflavin species that transfers a single atom of molecular oxygen to an organic substrate. Here we report that the bacterial flavoenzyme EncM catalyses the peroxyflavin-independent oxygenation-dehydrogenation dual oxidation of a highly reactive poly(β-carbonyl). The crystal structure of EncM with bound substrate mimics and isotope labelling studies reveal previously unknown flavin redox biochemistry. We show that EncM maintains an unexpected stable flavin-oxygenating species, proposed to be a flavin-N5-oxide, to promote substrate oxidation and trigger a rare Favorskii-type rearrangement that is central to the biosynthesis of the antibiotic enterocin. This work provides new insight into the fine-tuning of the flavin cofactor in offsetting the innate reactivity of a polyketide substrate to direct its efficient electrocyclization. PubMed: 24162851DOI: 10.1038/nature12643 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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