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首页> 外文期刊>Biochemistry >Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis
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Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis

机译：来自加拿大甲虫Dendroides canadensis越冬幼虫的抗冻蛋白中二硫键的定位

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摘要

Antifreeze proteins (AFPs) have been identified in certain high-latitude marine fish, insects and other terrestrial arthropods, and plants. Despite considerable structural variation, the mechanisms of their noncolligative antifreeze activity are probably quite similar. AFPs hydrogen bond onto the surface of potential seed ice crystals at preferred growth sites, thereby preventing growth of the crystals. AFPs from overwintering larvae of the beetle Dendroides canadensis are among the most active AFPs. These 8.7-kDa proteins consist of seven 12- or 13-mer repeating units. Their most striking feature is the location of cysteines every six residues throughout their length. Consequently, identification of the disulfide linkages of these cysteines is essential to understanding the structure of these AFPs, This study demonstrated that all of the 16 Cys residues in the Dendroides AFPs are disulfide bridged. All of the seven 12- or 13-mer repeats have internal disulfide bridges, and in all but the first repeat the Cys residues at positions 1 and 7 of the repeats are linked. In repeat 1 the Cys at position 1 is linked to the Cys at position 10, rather than the Cys at position 7 as in the other repeats, and the Cys at position 7 of the first repeat is linked to a Cys at position 4 of the second repeat. The disulfide bridges probably function to position the hydrophilic side chains of serine and threonine residues so that they hydrogen bond with ice. [References: 28]
机译：在某些高纬度海鱼，昆虫和其他陆生节肢动物和植物中已鉴定出防冻蛋白（AFP）。尽管结构上有相当大的变化，但其非协同防冻活性的机制可能非常相似。 AFP将氢键合到潜在生长晶种晶体的首选生长部位，从而阻止了晶体的生长。来自甲虫Dendroides canadensis越冬幼虫的AFP是最活跃的AFP。这些8.7 kDa蛋白由七个12-或13-mer重复单元组成。它们最显着的特征是半胱氨酸在其整个长度上每六个残基的位置。因此，鉴定这些半胱氨酸的二硫键对于理解这些AFP的结构是必不可少的。这项研究表明，树突状AFP中的所有16个Cys残基都是通过二硫键桥接的。七个12-或13-mer重复序列中的所有均具有内部二硫键，除第一个重复序列外，所有重复序列中1和7位的Cys残基均相连。在重复序列1中，位置1的Cys与位置10的Cys相连，而不是像其他重复序列中的位置7的Cys，而第一个重复序列的位置7的Cys与该序列的位置4的Cys相连。第二次重复。二硫键可能起到定位丝氨酸和苏氨酸残基亲水侧链的作用，从而使它们与冰形成氢键。 [参考：28]

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