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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Role of loop dynamics in thermal stability of mesophilic and thermophilic adenylosuccinate synthetase: a molecular dynamics and normal mode analysis study.
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Role of loop dynamics in thermal stability of mesophilic and thermophilic adenylosuccinate synthetase: a molecular dynamics and normal mode analysis study.

机译：回路动力学在嗜温和嗜热腺苷酸琥珀酸合成酶的热稳定性中的作用：分子动力学和正常模式分析研究。

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摘要

Enzymes from thermophiles are poorly active at temperatures at which their mesophilic homologs exhibit high activity and attain corresponding active states at high temperatures. In this study, comparative molecular dynamics (MD) simulations, supplemented by normal mode analysis, have been performed on an enzyme Adenylosuccinate synthetase (AdSS) from E. coli (mesophilic) and P. horikoshii (thermophilic) systems to understand the effects of loop dynamics on thermal stability of AdSS. In mesophilic AdSS, both ligand binding and catalysis are facilitated through the coordinated movement of five loops on the protein. The simulation results suggest that thermophilic P. horikoshii preserves structure and catalytic function at high temperatures by using the movement of only a subset of loops (two out of five) for ligand binding and catalysis unlike its mesophilic counterpart in E. coli. The pre-arrangement of the catalytic residues in P. horikoshii is well-preserved and salt bridges remain stable at high temperature (363K). The simulations suggest a general mechanism (including pre-arrangement of catalytic residues, increased polar residue content, stable salt bridges, increased rigidity, and fewer loop movements) used by thermophilic enzymes to preserve structure and be catalytically active at elevated temperatures.
机译：来自嗜热菌的酶在其嗜温同源物表现出高活性并在高温下达到相应的活性状态的温度下活性较差。在这项研究中，已对大肠杆菌（中温）和horikoshii（嗜热）系统的腺苷酸琥珀酸合成酶（AdSS）进行了比较分子动力学（MD）模拟，并辅以正常模式分析，以了解环的影响AdSS热稳定性的动力学。在嗜温AdSS中，通过蛋白质上五个环的协调运动，配体结合和催化都得到了促进。模拟结果表明，与大肠杆菌中的嗜温对应物不同，嗜热毕赤酵母通过仅利用一部分环（五分之二）进行配体结合和催化来保留高温下的结构和催化功能。 rik虫中催化残基的预先排列保存完好，盐桥在高温（363K）下保持稳定。模拟结果表明嗜热酶可使用一种通用机制（包括催化残基的预先排列，极性残基含量的增加，稳定的盐桥，增加的刚性和更少的环运动）来保护结构并在高温下具有催化活性。

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