4KRH

SeMet Haemonchus contortus Phosphoethanolamine N-methyltransferase 2 in complex with S-adenosyl-L-methionine

4KRH の概要

• エントリーDOI: 10.2210/pdb4krh/pdb
• 関連するPDBエントリー: 4KRG 4KRI
• 分子名称: Phosphoethanolamine N-methyltransferase 2, S-ADENOSYLMETHIONINE (2 entities in total)
• 機能のキーワード: methyltransferase, transferase
• 由来する生物種: Haemonchus contortus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 100889.16

構造登録者

Lee, S.G.,Jez, J.M. (登録日: 2013-05-16, 公開日: 2013-09-25, 最終更新日: 2024-11-20)

主引用文献

Lee, S.G.,Jez, J.M.
Evolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.
Structure, 21:1778-1787, 2013

PubMed Abstract: The phosphobase methylation pathway is the major route for supplying phosphocholine to phospholipid biosynthesis in plants, nematodes, and Plasmodium. In this pathway, phosphoethanolamine N-methyltransferase (PMT) catalyzes the sequential methylation of phosphoethanolamine to phosphocholine. In the PMT, one domain (MT1) catalyzes methylation of phosphoethanolamine to phosphomonomethylethanolamine and a second domain (MT2) completes the synthesis of phosphocholine. The X-ray crystal structures of the di-domain PMT from the parasitic nematode Haemonchus contortus (HcPMT1 and HcPMT2) reveal that the catalytic domains of these proteins are structurally distinct and allow for selective methylation of phosphobase substrates using different active site architectures. These structures also reveal changes leading to loss of function in the vestigial domains of the nematode PMT. Divergence of function in the two nematode PMTs provides two distinct antiparasitic inhibitor targets within the same essential metabolic pathway. The PMTs from nematodes, plants, and Plasmodium also highlight adaptable metabolic modularity in evolutionarily diverse organisms.

PubMed: 24012478
DOI: 10.1016/j.str.2013.07.023

実験手法

X-RAY DIFFRACTION (3 Å)