6RS4
Structure of tabersonine synthase - an alpha-beta hydrolase from Catharanthus roseus
Summary for 6RS4
Entry DOI | 10.2210/pdb6rs4/pdb |
Descriptor | Tabersonine synthase, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | alkaloid, tabersonine, natural product, biosynthesis, alpha/beta hydrolase fold, hydrolase |
Biological source | Catharanthus roseus (Madagascar periwinkle) |
Total number of polymer chains | 2 |
Total formula weight | 73194.85 |
Authors | Caputi, L.,Franke, J.,Bussey, K.,Farrow, S.C.,Curcino Vieira, I.J.,Stevenson, C.E.M.,Lawson, D.M.,O'Connor, S.E. (deposition date: 2019-05-21, release date: 2020-03-04, Last modification date: 2024-01-24) |
Primary citation | Caputi, L.,Franke, J.,Bussey, K.,Farrow, S.C.,Vieira, I.J.C.,Stevenson, C.E.M.,Lawson, D.M.,O'Connor, S.E. Structural basis of cycloaddition in biosynthesis of iboga and aspidosperma alkaloids. Nat.Chem.Biol., 16:383-386, 2020 Cited by PubMed Abstract: Cycloaddition reactions generate chemical complexity in a single step. Here we report the crystal structures of three homologous plant-derived cyclases involved in the biosynthesis of iboga and aspidosperma alkaloids. These enzymes act on the same substrate, named angryline, to generate three distinct scaffolds. Mutational analysis reveals how these highly similar enzymes control regio- and stereo-selectivity. PubMed: 32066966DOI: 10.1038/s41589-019-0460-x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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