6E1J

Crystal Structure of Methylthioalkylmalate Synthase (BjuMAM1.1) from Brassica juncea

6E1J の概要

• エントリーDOI: 10.2210/pdb6e1j/pdb
• 分子名称: 2-isopropylmalate synthase, A genome specific 1, MANGANESE (II) ION, 4-(METHYLSULFANYL)-2-OXOBUTANOIC ACID, ... (5 entities in total)
• 機能のキーワード: x-ray crystal structure, enzyme, methylthioalkylmalate synthase, plant protein
• 由来する生物種: Brassica juncea (Indian mustard)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112906.11

構造登録者

Lee, S.G.,Jez, J.M. (登録日: 2018-07-09, 公開日: 2019-05-08, 最終更新日: 2024-10-30)

主引用文献

Kumar, R.,Lee, S.G.,Augustine, R.,Reichelt, M.,Vassao, D.G.,Palavalli, M.H.,Allen, A.,Gershenzon, J.,Jez, J.M.,Bisht, N.C.
Molecular Basis of the Evolution of Methylthioalkylmalate Synthase and the Diversity of Methionine-Derived Glucosinolates.
Plant Cell, 31:1633-1647, 2019

PubMed Abstract: The globally cultivated species possess diverse aliphatic glucosinolates, which are important for plant defense and animal nutrition. The committed step in the side chain elongation of methionine-derived aliphatic glucosinolates is catalyzed by methylthioalkylmalate synthase, which likely evolved from the isopropylmalate synthases of leucine biosynthesis. However, the molecular basis for the evolution of methylthioalkylmalate synthase and its generation of natural product diversity in is poorly understood. Here, we show that genomes encode multiple methylthioalkylmalate synthases that have differences in expression profiles and 2-oxo substrate preferences, which account for the diversity of aliphatic glucosinolates across accessions. Analysis of the 2.1 Å resolution x-ray crystal structure of methylthioalkylmalate synthase identified key active site residues responsible for controlling the specificity for different 2-oxo substrates and the determinants of side chain length in aliphatic glucosinolates. Overall, these results provide the evolutionary and biochemical foundation for the diversification of glucosinolate profiles across globally cultivated species, which could be used with ongoing breeding strategies toward the manipulation of beneficial glucosinolate compounds for animal health and plant protection.

PubMed: 31023839
DOI: 10.1105/tpc.19.00046

実験手法

X-RAY DIFFRACTION (2.096 Å)