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A linker of the proline-threonine repeating motif sequence is bimodal.
Journal of Molecular Modeling ( IF 2.2 ) Pub Date : 2020-06-19 , DOI: 10.1007/s00894-020-04434-0
Munir Salomão Skaf 1 , Igor Polikarpov 2 , Ivana M Stanković 1, 3
Affiliation  

The linker of the endoglucanase from Xanthomonas campestris pv. campestris ((PT)12) has a specific sequence, a repeating proline-threonine motif. In order to understand its role, it has been compared to a regular sequence linker, in this work—the cellobiohydrolase 2 from Trichoderma reesei (CBH2). Elastic properties of the two linkers have been estimated by calculating free energy profile along the linker length from an enhanced sampling molecular dynamics simulation. The (PT)12 exhibits more pronounced elastic behaviour than CBH2. The PT repeating motif results in a two-mode energy profile which could be very useful in the enzyme motions along the substrate during hydrolytic catalysis.

中文翻译:

脯氨酸-苏氨酸重复基序序列的接头是双峰的。

Xanthomonas campestris pv的内切葡聚糖酶的接头campestris((PT)12)具有特定的序列,重复的脯氨酸-苏氨酸基序。为了理解其作用,在这项工作中将其与常规序列接头进行了比较-来自里氏木霉Trichoderma reesei)的纤维二糖水解酶2 (CBH2)。通过从增强的采样分子动力学模拟计算沿着接头长度的自由能分布,可以估算出两个接头的弹性性质。(PT)12表现出比CBH2更明显的弹性行为。PT重复基序产生双模式能量分布,这在水解催化过程中沿底物的酶运动中可能非常有用。
更新日期:2020-06-19
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