Download MendeleyStructures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Zubieta, C., He, X.Z., Dixon, R.A., Noel, J.P.(2001) Nat Struct Biol 8: 271-279
- PubMed: 11224575
- DOI: https://doi.org/10.1038/85029
- Primary Citation of Related Structures:
1FP1, 1FP2, 1FPQ, 6CIG - PubMed Abstract:
Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.
- Structural Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
Organizational Affiliation:
