4EMS

Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum

4EMS の概要

• エントリーDOI: 10.2210/pdb4ems/pdb
• 関連するPDBエントリー: 4E70
• 分子名称: Coniferyl alcohol 9-O-methyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: rossmann fold, dimer, transferase, small molecule o-methyltransferase, s-adenosyl-l-methionine, coniferyl alcohol, phenylpropanoid, methylation
• 由来する生物種: Linum nodiflorum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87311.45

構造登録者

Wolters, S.,Heine, A.,Petersen, M. (登録日: 2012-04-12, 公開日: 2013-05-01, 最終更新日: 2024-02-28)

主引用文献

Wolters, S.,Neeb, M.,Berim, A.,Schulze Wischeler, J.,Petersen, M.,Heine, A.
Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.
Acta Crystallogr.,Sect.D, 69:888-900, 2013

PubMed Abstract: Coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum (Linaceae) catalyzes the unusual methylation of the side-chain hydroxyl group of coniferyl alcohol. The protein was heterologously expressed in Escherichia coli as a hexahistidine derivative and purified for crystallization. Diffracting crystals were obtained of the pure protein and of its selenomethionine derivative, as well as of complexes with coniferyl alcohol and with S-adenosyl-L-homocysteine together with coniferyl alcohol 9-O-methyl ether (PDB entries 4ems, 4e70 and 4evi, respectively). The X-ray structures show that the phenylpropanoid binding mode differs from other phenylpropanoid O-methyltransferases such as caffeic acid O-methyltransferase. Moreover, the active site lacks the usually conserved and catalytic histidine residue and thus implies a different reaction mode for methylation. Site-directed mutagenesis was carried out to identify critical amino acids. The binding order of coniferyl alcohol and S-adenosyl-L-methionine was investigated by isothermal titration calorimetry experiments.

PubMed: 23633600
DOI: 10.1107/S0907444913002874

実験手法

X-RAY DIFFRACTION (1.7534 Å)