决定酯酶热适应性的结构特征

Protein Engineering, Design and Selection Pub Date : 2016-02-01 Epub Date: 2015-12-07 DOI:10.1093/protein/gzv061
Filip Kovacic, Agathe Mandrysch, Chetan Poojari, Birgit Strodel, Karl-Erich Jaeger
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引用次数: 0

摘要

微生物要适应极端的生活温度,就必须进化出在这些条件下具有高催化效率的酶。这种嗜极酶是研究蛋白质稳定性、动力学和功能之间关系的宝贵工具。尽管如此,人们对温度对酶的结构和功能的多重影响在分子水平上仍然知之甚少。我们对从生活在 10°C 至 70°C 温度范围内的细菌中分离出来的四种同源酯酶进行了分析,发现了通过优化蛋白质表面的局部柔韧性来调节蛋白质热特性的适应途径。虽然重组酯酶的生化特性保持不变,但它们的热特性已经进化到类似于各自细菌栖息地的特性。在酶催化的最佳温度附近进行的分子动力学模拟显示,四个表面暴露环的灵活性与温度有关。一些环路的灵活性随着温度的升高而增加,随着温度的降低而降低,这与那些有助于蛋白质稳定性的环路所预期的一样。这些区域保持灵活性似乎对酶的正常功能很重要。远离活性位点的这四个环的结构差异远远大于整个蛋白质结构的差异,这表明这些环内的氨基酸交换更为频繁,从而使细菌能够根据不同的温度要求调整原子间的相互作用,而不影响酶的整体功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structural features determining thermal adaptation of esterases.

The adaptation of microorganisms to extreme living temperatures requires the evolution of enzymes with a high catalytic efficiency under these conditions. Such extremophilic enzymes represent valuable tools to study the relationship between protein stability, dynamics and function. Nevertheless, the multiple effects of temperature on the structure and function of enzymes are still poorly understood at the molecular level. Our analysis of four homologous esterases isolated from bacteria living at temperatures ranging from 10°C to 70°C suggested an adaptation route for the modulation of protein thermal properties through the optimization of local flexibility at the protein surface. While the biochemical properties of the recombinant esterases are conserved, their thermal properties have evolved to resemble those of the respective bacterial habitats. Molecular dynamics simulations at temperatures around the optimal temperatures for enzyme catalysis revealed temperature-dependent flexibility of four surface-exposed loops. While the flexibility of some loops increased with raising the temperature and decreased with lowering the temperature, as expected for those loops contributing to the protein stability, other loops showed an increment of flexibility upon lowering and raising the temperature. Preserved flexibility in these regions seems to be important for proper enzyme function. The structural differences of these four loops, distant from the active site, are substantially larger than for the overall protein structure, indicating that amino acid exchanges within these loops occurred more frequently thereby allowing the bacteria to tune atomic interactions for different temperature requirements without interfering with the overall enzyme function.

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