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

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

Experimental method

X-RAY DIFFRACTION (2.19 Å)