This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fpq
From Proteopedia
|
CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE
Overview
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.
About this Structure
1FPQ is a Single protein structure of sequence from Medicago sativa with SAM as ligand. Full crystallographic information is available from OCA.
Reference
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases., Zubieta C, He XZ, Dixon RA, Noel JP, Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575
Page seeded by OCA on Tue Nov 20 15:08:01 2007
