Wang Shizhen, Ma Chengwei, Zeng An-Ping
Department of Chemical and Biochemical Engineering College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China.
Institute of Bioprocess and Biosystems Engineering Hamburg University of Technology Hamburg Germany.
Eng Life Sci. 2021 Mar 2;21(5):314-323. doi: 10.1002/elsc.202000065. eCollection 2021 May.
Conformational change associated with allosteric regulation in a protein is ultimately driven by energy transformation. However, little is known about the latter process. In this work, we combined steered molecular dynamics simulations and sequence conservation analysis to investigate the conformational changes and energy transformation in the allosteric enzyme aspartokinase III (AK III) from . Correlation analysis of energy change at residue level indicated significant transformation between electrostatic energy and dihedral angle energy during the allosteric regulation. Key amino acid residues located in the corresponding energy transduction pathways were identified by dynamic energy correlation analysis. To verify their functions, residues with a high energy correlation in the pathways were altered and their effects on allosteric regulation of AKIII were determined. This study sheds new insights into energy transformation during allosteric regulation of AK III and proposes a strategy to identify key residues that are involved in intramolecular energy transduction and thus in driving the allosteric process.
蛋白质中与变构调节相关的构象变化最终由能量转换驱动。然而，对于后一过程知之甚少。在这项工作中，我们结合了引导分子动力学模拟和序列保守性分析，以研究来自[具体来源未给出]的变构酶天冬氨酸激酶III（AK III）中的构象变化和能量转换。残基水平的能量变化相关性分析表明，在变构调节过程中静电能和二面角能之间存在显著转换。通过动态能量相关性分析确定了位于相应能量转导途径中的关键氨基酸残基。为了验证它们的功能，改变了途径中具有高能量相关性的残基，并确定了它们对AKIII变构调节的影响。这项研究为AK III变构调节过程中的能量转换提供了新的见解，并提出了一种策略来识别参与分子内能量转导从而驱动变构过程的关键残基。
