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首页> 外文期刊>The protein journal >The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase.
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The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase.

机译：在人谷胱甘肽合成酶的二聚体界面上强静电相互作用的作用。

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摘要

The obligate homodimer human glutathione synthetase (hGS) provides an ideal system for exploring the role of protein-protein interactions in the structural stability, activity and allostery of enzymes. The two active sites of hGS, which are 40 ? apart, display allosteric modulation by the substrate γ-glutamylcysteine (γ-GC) during the synthesis of glutathione, a key cellular antioxidant. The two subunits interact at a relatively small dimer interface dominated by electrostatic interactions between S42, R221, and D24. Alanine scans of these sites result in enzymes with decreased activity, altered γ-GC affinity, and decreased thermal stability. Molecular dynamics simulations indicate these mutations disrupt interchain bonding and impact the tertiary structure of hGS. While the ionic hydrogen bonds and salt bridges between S42, R221, and D24 do not mediate allosteric communication in hGS, these interactions have a dramatic impact on the activity and structural stability of the enzyme.
机译：专性的同型二聚体人谷胱甘肽合成酶（hGS）为探索蛋白质间相互作用在酶的结构稳定性，活性和变构性中的作用提供了理想的系统。 hGS的两个活性位点是40？。另外，在关键细胞抗氧化剂谷胱甘肽的合成过程中，底物γ-谷氨酰半胱氨酸（γ-GC）表现出变构调节。两个亚基在相对较小的二聚体界面相互作用，该二聚体界面主要受S42，R221和D24之间的静电相互作用影响。对这些位点进行丙氨酸扫描会导致酶活性降低，γ-GC亲和力降低和热稳定性降低。分子动力学模拟表明这些突变破坏链间键合并影响hGS的三级结构。尽管S42，R221和D24之间的离子氢键和盐桥不介导hGS中的变构通讯，但这些相互作用对酶的活性和结构稳定性有重大影响。

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