7e22

Crystal structure of two pericyclases catalyzing [4+2] cycloaddition

spinqualitylabelsall models 7e22, resolution 2.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7e22 is a 1 chain structure with sequence from Fusarium sp. FN080326. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.63Å Ligands: HVF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FSA2_FUSSF Diels-Alderase; part of the gene cluster that mediates the biosynthesis of equisetin and fusarisetin A, 2 trans-fused decalin-containing tetramic acids with antimicrobial activity (PubMed:25770422). The PKS module of fsa1 together with the enoylreductase fsa3 catalyze the formation of the polyketide unit which is then conjugated to L-serine by the condensation domain of the fsa1 NRPS module (PubMed:25770422). Activity of the Dieckmann cyclase domain (RED) results in release of the intermediate N-desmethylequisetin also called trichosetin (PubMed:25770422). Diels-Alderase fsa2 is involved in endo-selective Diels-Alder cycloaddition to form the decalin ring of equisetin (PubMed:25770422, PubMed:28401214). Subsequent N-methylation is carried out by fsa4 to give equisetin (PubMed:25770422). The enzymatic gene responsible for the conversion of equisetin to fusarisetin A has not been identified yet and is probably located outside of the fsa cluster (PubMed:28401214).

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