Conservation and divergence on plant seed 11S globulins based on crystal structures
Conservation and divergence on plant seed 11S globulins based on crystal structures
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DOI：
10.1016/j.bbapap.2010.02.016
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发表时间：
2010-07-01
影响因子：
3.2
通讯作者：
Maruyama, Nobuyuki
中科院分区：
文献类型：
--
作者：
Tandang-Silvas, Mary Rose G.;Fukuda, Takako;Maruyama, Nobuyuki
本文介绍了菜籽原十字花素和豌豆原蛋白两种原11s球蛋白的晶体结构。我们已经将它们与其他已知的植物种子11S和75球蛋白的结构进行了广泛的比较。总的来说，11S球蛋白晶体结构中的无序区与它们的五个可变区相对应。前十字花素可变区i相对较短，呈环状构象。这个区域在其他的前11s球蛋白晶体中是高度无序的。尽管整体结构保持不变，但在整个群体中也会发生局部的螺旋和链变异。我们展示了这些变化如何改变特定的物理化学、功能和生理特性。分子表面的脂肪族疏水残基与球蛋白的T-m值密切相关。我们还考虑了据报道影响热稳定性的其他结构特征，但没有得出明确的结论，因为每个因素都有加或减的作用。proA3B4与成熟A3B4的比较显示，在可变区域II和IV附近的rm.s.d.值增加，这两个区域都在IE面上。对115和75个球蛋白进行二级结构比对，发现16个相同的残基。基于proA3B4序列，Pro60、Gly128、Phe163、Phe208、Leu213、Leu227、Ile237、Pro382、Val404、Pro425和Val 466参与三聚体的形成和稳定。Gly28, Gly74, Asp135， Gly349和Gly397参与正确的球状折叠。(C) 2010 Elsevier B.V.版权所有
The crystal structures of two pro-11S globulins namely: rapeseed procruciferin and pea prolegumin are presented here. We have extensively compared them with the other known structures of plant seed 11S and 75 globulins. In general, the disordered regions in the crystal structures among the 11S globulins correspond to their five variable regions. Variable region Ill of procruciferin is relatively short and is in a loop conformation. This region is highly disordered in other pro-11S globulin crystals. Local helical and strand variations also occur across the group despite general structure conservation. We showed how these variations may alter specific physicochemical, functional and physiological properties. Aliphatic hydrophobic residues on the molecular surface correlate well with T-m values of the globulins. We also considered other structural features that were reported to influence thermal stability but no definite conclusion was drawn since each factor has additive or subtractive effect. Comparison between proA3B4 and mature A3B4 revealed an increase in r.m.s.d. values near variable regions II and IV. Both regions are on the IE face. Secondary structure based alignment of 115 and 75 globulins revealed 16 identical residues. Based on proA3B4 sequence, Pro60, Gly128, Phe163, Phe208, Leu213, Leu227, Ile237, Pro382, Val404, Pro425 and Val 466 are involved in trimer formation and stabilization. Gly28, Gly74, Asp135, Gly349 and Gly397 are involved in correct globular folding. (C) 2010 Elsevier B.V. All rights reserved.