Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability:: Lessons from structural genomics of Thermotoga maritima
Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability:: Lessons from structural genomics of Thermotoga maritima
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DOI：
10.1016/j.jmb.2005.11.065
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发表时间：
2006-02-17
影响因子：
5.6
通讯作者：
Godzik, A
中科院分区：
文献类型：
--
作者：
Robinson-Rechavi, M;Alibés, A;Godzik, A
对蛋白质热稳定性的结构基础的研究产生了一幅令人困惑的图景。已经分析了来自各种嗜热物种的少量蛋白质，表明不同的结构特征对蛋白质的热稳定性负责。利用结构基因组学的最新进展，我们编制了一个相对较大的蛋白质结构数据集，该数据库是非常仔细和有选择地构建的；即，该数据集仅包含来自一个特定生物体的蛋白质的实验确定的结构，即高温嗜热菌Thermotoga maritima的蛋白质结构，以及来自中嗜热细菌的密切同源物的结构。与以前的研究结论相比，我们的分析表明齐聚顺序、氢键和二级结构在细菌适应高嗜热性方面起到的作用不大。另一方面，数据显示盐桥的密度和毛滴虫蛋白质的致密性都有非常显著的增加。后一种影响可以通过接触顺序或溶剂可及性来衡量，网络分析显示这种嗜热菌中高连接残基的具体增加。这些特征解释了96%所研究的蛋白质对的变化。我们的结果为蛋白质在一个物种中的热稳定性提供了一个清晰的图景，并为未来热适应研究提供了一个框架。(C)2005爱思唯尔有限公司。保留所有权利。
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. (c) 2005 Elsevier Ltd. All rights reserved.