9SRP
Structure of the Diels-Alderase ChlE3 in complex with cofactor FAD
Summary for 9SRP
| Entry DOI | 10.2210/pdb9srp/pdb |
| Descriptor | ChlE3, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | diels-alderase, spirotetronate, chlorothricin, oxidoreductase |
| Biological source | Streptomyces antibioticus |
| Total number of polymer chains | 4 |
| Total formula weight | 216156.75 |
| Authors | Manzo-Ruiz, M.B.,Back, C.R.,Race, P.R. (deposition date: 2025-09-24, release date: 2026-06-24, Last modification date: 2026-07-15) |
| Primary citation | Devine, A.J.,Manzo-Ruiz, M.,Back, C.R.,Zorn, K.,Hayes, M.A.,Race, P.R.,Willis, C.L. Creating molecular complexity in the chemoenzymatic synthesis of chlorothricin analogues using tandem Diels-Alderases. Org.Biomol.Chem., 24:5457-5464, 2026 Cited by PubMed Abstract: Chlorothricin is a polyketide-derived natural product isolated from . It possesses an elaborate pentacyclic aglycone core which incorporates a spirotetronic acid moiety, linked to a -decalin system, embedded within a macrocycle. Using synthetic substrate analogues and purified recombinant proteins, here we demonstrate that assembly of this scaffold proceeds sequential biocatalytic Diels-Alder reactions, promoted by the enzymes ChlE3 and ChlL. Both Diels-Alderases exhibit sufficiently relaxed substrate selectivity to facilitate access to non-natural chlorothricin analogues biotransformations. The X-ray crystal structure of ChlE3 reveals the molecular basis of decalin formation by this enzyme. Harnessing this enzymatic cascade in biocatalysis could provide a valuable biomimetic route to both natural and non-natural spirotetronates, and the work described herein lays the foundation for application of these enzymes in chemoenzymatic syntheses of complex products. PubMed: 42306997DOI: 10.1039/d6ob00728g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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