4LEJ

Crystal Structure of the Korean pine (Pinus koraiensis) vicilin

4LEJ の概要

• エントリーDOI: 10.2210/pdb4lej/pdb
• 分子名称: Vicilin, COPPER (II) ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: seed storage protein, allergen, cupin, seed storage, plant protein
• 由来する生物種: Pinus koraiensis (channamu)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46502.06

構造登録者

Jin, T.C.,Wang, Y.,Zhang, Y.Z. (登録日: 2013-06-25, 公開日: 2014-01-22, 最終更新日: 2024-02-28)

主引用文献

Jin, T.,Wang, Y.,Chen, Y.W.,Fu, T.J.,Kothary, M.H.,McHugh, T.H.,Zhang, Y.
Crystal Structure of Korean Pine ( Pinus koraiensis ) 7S Seed Storage Protein with Copper Ligands.
J.Agric.Food Chem., 62:222-228, 2014

PubMed Abstract: The prevalence of food allergy has increased in recent years, and Korean pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean pine vicilin purified from raw pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean pine vicilin at 2.40 Å resolution. The overall structure of pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, including peanut and soybean. Additional studies are needed to assess whether the copper-coordinating property of vicilins has a biological function in the relevant plants. The nutritional value of this copper-coordinating protein in tree nuts and other edible seeds may be worth further investigations.

PubMed: 24328105
DOI: 10.1021/jf4039887

実験手法

X-RAY DIFFRACTION (2.402 Å)