6RT8

Structure of catharanthine synthase - an alpha-beta hydrolase from Catharanthus roseus with a cleaviminium intermediate bound

Summary for 6RT8

Entry DOI	10.2210/pdb6rt8/pdb
Descriptor	Catharanthine synthase, 18-carboxymethoxy-cleaviminium, HEXAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywords	alkaloid, catharanthine, natural product, biosynthesis, alpha/beta hydrolase fold, hydrolase
Biological source	Catharanthus roseus (Madagascar periwinkle)
Total number of polymer chains	8
Total formula weight	300444.46
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: 2019-05-22, 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: 32066966 DOI: 10.1038/s41589-019-0460-x PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.19 Å)

Structure validation