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Purification crystallization and preliminary X-ray analysis of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli

机译:大肠杆菌异柠檬酸脱氢酶激酶/磷酸酶的纯化结晶和初步X射线分析

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摘要

The Escherichia coli aceK gene encodes isocitrate dehydrogenase kinase/phosphatase (EC 2.7.11.5), a bifunctional protein that phosphorylates and dephosphorylates isocitrate dehydrogenase (IDH), resulting in its inactivation and activation, respectively. This reversible (de)phosphorylation directs iso­citrate, an intermediate of the citric acid cycle, to either go through the full cycle or to enter the glyoxylate bypass. In the present study, the AceK protein from E. coli has been purified and crystallized. Three crystal forms were obtained from very similar crystallization conditions. The crystals belong to space groups P41212, P3221 and P212121 and diffracted X-rays to resolutions of 2.9, 3.0 and 2.7 Å, respectively.
机译:大肠杆菌aceK基因编码异柠檬酸脱氢酶激酶/磷酸酶(EC 2.7.11.5),这是一种双功能蛋白,可将异柠檬酸脱氢酶(IDH)磷酸化和去磷酸化,从而分别使其失活和活化。这种可逆的(去)磷酸化作用可引导柠檬酸循环的中间产物异柠檬酸通过整个循环或进入乙醛酸旁路。在本研究中,来自大肠杆菌的AceK蛋白已被纯化和结晶。从非常相似的结晶条件获得了三种晶型。晶体属于空间群P41212,P3221和P212121,并且衍射的X射线分别具有2.9、3.0和2.7Å的分辨率。

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