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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer
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Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer

机译：大豆11S球蛋白的晶体结构：大豆球蛋白A3B4同六聚体

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摘要

Most plant seeds contain 11S globulins as major storage proteins for their nutrition. Soybean glycinin belongs to the 11 S globulin family and consists of five kinds of subunits. We determined the crystal structure of a homohexamer of the glycinin A3B4 subunit at 2.1-Angstrom resolution. The crystal structure shows that the hexamer has 32-point group symmetry formed by face-to-face stacking of two trimers. The interface buries the highly conserved interchain disulfide. Based on the structure, we propose that an ingenious face-to-face mechanism controls the hexamer formation of the 11 S globulin by movement of a mobile disordered region to the side of the trimer after posttranslational processing. Electrostatic analysis of the faces suggests that the interchain disulfide-containing face has high positive potential at acidic pH, which induces dissociation of the hexamer into trimers that may be susceptible to proteinases after seed imbibition. This dissociation might result in the degradation and mobilization of 11S globulins as storage proteins in embryos during germination and seedling growth. [References: 25]
机译：大多数植物种子都含有11S球蛋白作为其营养的主要存储蛋白。大豆大豆球蛋白属于11 S球蛋白家族，由5种亚基组成。我们确定了甘氨酸A3B4亚基的同六聚体的晶体结构，分辨率为2.1埃。晶体结构表明该六聚体具有通过两个三聚体的面对面堆叠而形成的32点基团对称性。该界面掩埋了高度保守的链间二硫键。基于该结构，我们提出了一种巧妙的面对面机制，通过在翻译后处理后将移动无序区域移至三聚体一侧来控制11 S球蛋白的六聚体形成。脸部的静电分析表明，含链间二硫键的脸部在酸性pH下具有较高的正电势，这会导致六聚体解离为三聚体，三聚体可能在种子吸收后易受蛋白酶的影响。这种解离可能会导致11S球蛋白在发芽和幼苗生长过程中降解并动员为胚胎中的贮藏蛋白。 [参考：25]

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