1FPQ

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

1FPQ の概要

• エントリーDOI: 10.2210/pdb1fpq/pdb
• 関連するPDBエントリー: 1FP1 1FP2 1FPX
• 分子名称: ISOLIQUIRITIGENIN 2'-O-METHYLTRANSFERASE, S-ADENOSYLMETHIONINE (3 entities in total)
• 機能のキーワード: selenomethionine substituted protein, transferase
• 由来する生物種: Medicago sativa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42280.01

構造登録者

Zubieta, C.,Dixon, R.A.,Noel, J.P. (登録日: 2000-08-31, 公開日: 2001-03-07, 最終更新日: 2024-11-13)

主引用文献

Zubieta, C.,He, X.Z.,Dixon, R.A.,Noel, J.P.
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Nat.Struct.Biol., 8:271-279, 2001

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.

PubMed: 11224575
DOI: 10.1038/85029

実験手法

X-RAY DIFFRACTION (2 Å)