3C3Y

Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum

3C3Y の概要

• エントリーDOI: 10.2210/pdb3c3y/pdb
• 分子名称: O-methyltransferase, CALCIUM ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: plant secondary metabolism, o-methyltransferase, transferase
• 由来する生物種: Mesembryanthemum crystallinum (common iceplant)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54126.03

構造登録者

Kopycki, J.G.,Rauh, D.,Neumann, P.,Stubbs, M.T. (登録日: 2008-01-29, 公開日: 2008-04-01, 最終更新日: 2026-02-11)

主引用文献

Kopycki, J.G.,Rauh, D.,Chumanevich, A.A.,Neumann, P.,Vogt, T.,Stubbs, M.T.
Biochemical and Structural Analysis of Substrate Promiscuity in Plant Mg(2+)-Dependent O-Methyltransferases
J.Mol.Biol., 378:154-164, 2008

PubMed Abstract: Plant S-adenosyl-l-methionine-dependent class I natural product O-methyltransferases (OMTs), related to animal catechol OMTs, are dependent on bivalent cations and strictly specific for the meta position of aromatic vicinal dihydroxy groups. While the primary activity of these class I enzymes is methylation of caffeoyl coenzyme A OMTs, a distinct subset is able to methylate a wider range of substrates, characterized by the promiscuous phenylpropanoid and flavonoid OMT. The observed broad substrate specificity resides in two regions: the N-terminus and a variable insertion loop near the C-terminus, which displays the lowest degree of sequence conservation between the two subfamilies. Structural and biochemical data, based on site-directed mutagenesis and domain exchange between the two enzyme types, present evidence that only small topological changes among otherwise highly conserved 3-D structures are sufficient to differentiate between an enzymatic generalist and an enzymatic specialist in plant natural product methylation.

PubMed: 18342334
DOI: 10.1016/j.jmb.2008.02.019

実験手法

X-RAY DIFFRACTION (1.371 Å)