首页> 外文期刊>Journal of Molecular Biology >Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.
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Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.

机译:豆科植物凝集素中金属结合与顺式/反式异构化之间的相互作用:安哥拉凝集素的结构和热力学研究。

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摘要

The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.
机译:研究了紫檀(Pterocarpus angolensis)的金属结合,碳水化合物结合活性,稳定性和凝集素结构之间的相互作用。去除金属会导致蛋白形式更加灵活,构象稳定性大大降低。这种无金属形式的晶体结构显示出显着的结构重排,尽管保留了一些允许糖结合的结构特征。我们建议,在豆类植物凝集素单体的C末端β链开始处替换天冬酰胺残基会阻碍顺肽键在脱金属后的反式异构化,并构成支配非-异构体状态的分子内开关。脯氨酸键和最终的凝集素表型。

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