首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Cloning crystallization and preliminary X-ray studies of XC2981 from Xanthomonas campestris a putative CutA1 protein involved in copper-ion homeostasis
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Cloning crystallization and preliminary X-ray studies of XC2981 from Xanthomonas campestris a putative CutA1 protein involved in copper-ion homeostasis

机译:Xanthomonas campestris XC2981的克隆结晶和初步X射线研究Xanthomonas campestris是一种参与铜离子稳态的推定CutA1蛋白。

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摘要

Divalent metal ions play key roles in all living organisms, serving as cofactors for many proteins involved in a variety of electron-transfer activities. However, copper ions are highly toxic when an excessive amount is accumulated in a cell. CutA1 is a protein found in all kingdoms of life that is believed to participate in copper-ion tolerance in Escherichia coli, although its specific function remains unknown. Several crystal structures of multimeric CutA1 with different rotation angles and degrees of interaction between trimer interfaces have been reported. Here, the cloning, expression, crystallization and preliminary X-ray analysis of XC2981, a possible CutA1 protein present in the plant pathogen Xanthomonas campestris, are reported. The XC2981 crystals diffracted to a resolution of 2.6 Å. They are cubic and belong to space group I23, with unit-cell parameters a = b = c = 130.73 Å.
机译:二价金属离子在所有活生物体中都起着关键作用,是参与多种电子转移活动的许多蛋白质的辅助因子。然而,当电池中积累过多的铜离子时,铜离子的毒性很高。 CutA1是一种在所有生命王国中发现的蛋白质,尽管其特定功能仍然未知,但据信它参与了大肠杆菌中的铜离子耐受性。已经报道了具有不同旋转角度和三聚体界面之间的相互作用度的多聚CutA1的几种晶体结构。在这里,报道了XC2981的克隆,表达,结晶和初步X射线分析,XC2981是存在于植物病原体Xanthomonas campestris中的一种可能的CutA1蛋白。 XC2981晶体衍射到2.6Å的分辨率。它们是立方的,属于I23空间组,单位像元参数a = b = c = 130.73Å。

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