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Crystal structure of soybean proglycinin alaB1b homotrimer

机译:大豆蛋白原大豆球蛋白alaB1b均三聚体的晶体结构

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摘要

Soybean glycinin is a member of the 11 S globulin family. The crystal structure of proglycinin was determined by X-ray crystallography at 2.8 Angstrom resolution with an R-factor of 0.199 and a free X-factor of 0.250. A trimer molecule was found in an asymmetric unit of crystals. The trimer model contains three A1aB1b subunits and comprises 1128 amino acid residues and 34 water molecules. The constituent protomers of the homo-trimeric protein are arranged around a 3-fold symmetry axis with dimensions of 95 Angstrom x 95 Angstrom x 40 A. The protomer model is composed of five fragments which correspond roughly to conserved regions based on the sequence alignment of various 11 S globulins. The core of the protomer consists of two jelly-roll beta -barrels and two extended helix domains. This structure of proglycinin is similar to those of canavalin and phaseolin belonging to the 7 S globulin family, strongly supporting the hypothesis that both 7 S and 11S globulins are derived from a common ancestor. The inter and intra-chain disulfide bonds conserved in the 11S globulin family are clearly observed. It is found that the face with the inter-chain disulfide bond (IE face) contains more hydrophobic residues than that with the intra-chain disulfide bond. This suggests that a mature hexamer is formed by the interaction between the IE faces after processing.
机译:大豆大豆球蛋白是11 S球蛋白家族的成员。原大豆球蛋白的晶体结构通过X射线晶体学以2.8埃的分辨率测定,R因子为0.199,游离X因子为0.250。在晶体的不对称单元中发现了三聚体分子。三聚体模型包含三个A1aB1b亚基,包含1128个氨基酸残基和34个水分子。同源三聚体蛋白质的组成原发子围绕一个3倍对称轴排列,尺寸为95埃x 95埃x 40A。该原发性模型由五个片段组成,这些片段大致基于保守序列的保守性而对应于保守区。各种11 S球蛋白。启动子的核心由两个果冻卷β桶和两个扩展的螺旋域组成。原大豆球蛋白的结构类似于属于7 S球蛋白家族的canavalin和菜豆蛋白的结构,强烈支持7 S和11S球蛋白均来自共同祖先的假设。清楚地观察到11S球蛋白家族中保守的链间和链内二硫键。发现具有链间二硫键的面(IE面)比具有链内二硫键的面含有更多的疏水残基。这表明通过加工后IE面之间的相互作用形成了成熟的六聚体。

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