生物信息学2016，Vol.14Issue(3)：139-145,7.DOI:10.3969/j.issn.1672-5565.2016.03.03
DnaK 蛋白扭链残基突变体影响其 ATPase 活性的分子动力学模拟研究
Using molecular dynamics simulation to study the effects of the ATPase activity in mutants of hinge residues of Dnak
摘要
Abstract
When the highly conserved hinge residues ( I202, S203, G223, L227, G228) , which are located in the subdomain II-A and II-B of NBD ( Nucleotide binding domain) in the E.coil’ s Dnak, mutate into alanine.It is not clear that the change reason of ATPase activity.We build all of the wild type and mutant protein model which contain small molecule ATP by using the method of homologous modeling, than using the molecular dynamics simulation ( MDs) to study the comformational change of these mutants, and want to find the relationship with the change of ATPase activity.Results show that the distances between the hydroxyl of Tyr 11 residue and the γphosphate of ATP in all models expect L227A have obvious rules with the activity of ATPase; but the change of compactness in β220 (214-221), which can impact the binding of DnaJ and effect the activity of ATPase, conform to the rules.The further experiment of protein docking confirm it, so the mutants of hinge residues may influence the ATPase activity by the changes of these two parts.关键词
DnaK/扭链残基/同源建模/分子动力学模拟/蛋白对接Key words
DnaK/Hinge residues/Homologous modeling/Molecular dynamics simulation/Protein docking分类
生物科学引用本文复制引用
张桥石,李灌澍,窦薛楷,薛友林,宋有涛..DnaK 蛋白扭链残基突变体影响其 ATPase 活性的分子动力学模拟研究[J].生物信息学,2016,14(3):139-145,7.基金项目
国家自然科学基金项目（31570154）；国家自然科学基金项目（31201285）。 （）
