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Protein dynamics of [Cu-Zn] superoxide dismutase (SOD1): How protein motions at the global and local levels impact the reactivity of SOD1.
Journal of Inorganic Biochemistry ( IF 3.9 ) Pub Date : 2020-06-24 , DOI: 10.1016/j.jinorgbio.2020.111161
Eamonn F Healy 1 , Rafael Flores 1 , Vincent M Lynch 2 , Santiago Toledo 1
Affiliation  

This work explores the pivotal role that protein mobility plays in facilitating the catalytic activity of Copper-Zinc superoxide dismutase (SOD1). Through both localized active site distortions and correlated domain movement, these motions enable the enzyme to adopt the conformations necessary to achieve both substrate delivery and efficient catalytic transformation. Structural and computational studies of a biomimetic model complex are used to probe the localized interactions between substrate and secondary sphere residues that play a role in guiding substrate to the active site, as well as facilitating the conformational changes necessary for substrate turnover. Normal mode analysis (NMA) of SOD1 demonstrates how collective domain motion influences key residues of the electrostatic loop (ESL), guiding substrate to the active site and facilitating the delivery of the conserved water network necessary for proton transfer.



中文翻译:

[Cu-Zn] 超氧化物歧化酶 (SOD1) 的蛋白质动力学:全局和局部水平的蛋白质运动如何影响 SOD1 的反应性。

这项工作探索了蛋白质迁移率在促进铜锌超氧化物歧化酶 (SOD1) 催化活性方面的关键作用。通过局部活性位点扭曲和相关域运动,这些运动使酶能够采用实现底物传递和有效催化转化所需的构象。仿生模型复合体的结构和计算研究用于探测底物和二级球体残基之间的局部相互作用,这些相互作用在引导底物到活性位点方面发挥作用,并促进底物周转所需的构象变化。SOD1 的正态模式分析 (NMA) 展示了集体域运动如何影响静电环 (ESL) 的关键残基,

更新日期:2020-06-30
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