Crystal structure of Korean pine (Pinus koraiensis) 7S seed storage protein with copper ligands.

Crystal structure of Korean pine (Pinus koraiensis) 7S seed storage protein with copper ligands.
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具有铜配体的红松 (Pinus koraiensis) 7S 种子储存蛋白的晶体结构。

DOI:
10.1021/jf4039887
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发表时间:
2014
影响因子:
6.1
通讯作者:
Zhang,Yuzhu
Zhang,Yuzhu
中科院分区:
农林科学1区
文献类型:
--
作者:
Jin,Tengchuan;Wang,Yang;Chen,Yu-Wei;Fu,Tong-Jen;Kothary,MahendraH;McHugh,TaraH;Zhang,Yuzhu

文献摘要

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近年来食物过敏的患病率呈上升趋势,红松豌豆毒素是一种潜在的食物过敏原。我们以前曾报道过从生松子中纯化红松豌豆球蛋白的结晶。在这里,我们报告的分离vicilin mRNA和红松vicilin在2.40 nm分辨率的晶体结构。松仁豌豆球蛋白的整体结构与其他7S种子贮藏蛋白的结构相似,由N-末端结构域和C-末端结构域组成。每个假设cupin倍,他们是对称的有关pseudodyad轴。三个豌豆球蛋白分子通过头对尾缔合形成甜甜圈形三聚体。红松坚果豌豆球蛋白的结构表征出乎意料地表明,在其天然三聚体状态下,豌豆球蛋白具有三个铜配体。序列比对表明,铜配位残基在南瓜,芝麻,番茄和几个树坚果中是保守的,而它们在一些豆类,包括花生和大豆中不保守。需要进一步的研究来评估是否铜的协调特性的Vicilins在相关植物的生物功能。这种铜配位蛋白在树坚果和其他可食用种子中的营养价值可能值得进一步研究。
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.