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Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima.

机译:静电相互作用,紧密度和四级结构对蛋白质热稳定性的贡献:来自滨海热菌的结构基因组学的教训。

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摘要

Studies of the structural basis of protein thermostability have produced a confusing picture. Small sets of proteins have been analyzed from a variety of thermophilic species, suggesting different structural features as responsible for protein thermostability. Taking advantage of the recent advances in structural genomics, we have compiled a relatively large protein structure dataset, which was constructed very carefully and selectively; that is, the dataset contains only experimentally determined structures of proteins from one specific organism, the hyperthermophilic bacterium Thermotoga maritima, and those of close homologs from mesophilic bacteria. In contrast to the conclusions of previous studies, our analyses show that oligomerization order, hydrogen bonds, and secondary structure play minor roles in adaptation to hyperthermophily in bacteria. On the other hand, the data exhibit very significant increases in the density of salt-bridges and in compactness for proteins from T.maritima. The latter effect can be measured by contact order or solvent accessibility, and network analysis shows a specific increase in highly connected residues in this thermophile. These features account for changes in 96% of the protein pairs studied. Our results provide a clear picture of protein thermostability in one species, and a framework for future studies of thermal adaptation.
机译:对蛋白质热稳定性的结构基础的研究产生了令人困惑的画面。已从各种嗜热菌种中分析了少量蛋白质,表明不同的结构特征是造成蛋白质热稳定性的原因。利用结构基因组学的最新进展,我们编译了一个相对较大的蛋白质结构数据集,该数据集非常仔细和选择性地构建。也就是说,数据集仅包含实验确定的一种特定生物体蛋白质的结构,即超嗜热细菌马氏嗜热菌,以及嗜温细菌的紧密同源物。与以前的研究结论相反,我们的分析表明,寡聚顺序,氢键和二级结构在适应细菌的超嗜热性方面起着较小的作用。另一方面,该数据显示来自盐生螺旋体的蛋白质的盐桥密度和紧密度显着增加。后者的影响可以通过接触顺序或溶剂的可及性来衡量,网络分析表明该嗜热剂中高度连接的残基有特定的增加。这些特征占所研究蛋白质对96%的变化。我们的结果为一个物种的蛋白质热稳定性提供了清晰的图像,并为将来的热适应性研究提供了框架。

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