首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum
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Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum

机译:谷氨酸棒杆菌中总氮调节剂AmtR的结晶和初步晶体学分析

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摘要

AmtR, a member of the TetR family of transcription regulators, is a global regulator of nitrogen control in Corynebacterium glutamicum. Unlike other TetR-family members, which are regulated by small-molecule effectors, AmtR is regulated by a protein called GlnK. It has been shown that a GlnK trimer has to become adenylylated prior to formation of a complex with AmtR. The physiological function of AmtR has been very well studied, but structural characterization of the mechanistic aspects of AmtR-regulated transcription has yet to be accomplished. AmtR has successfully been crystallized in space group P21212, with six molecules in the asymmetric unit and unit-cell parameters a = 153.34, b = 163.10, c = 51.93 Å. Preliminary phases were obtained using Se-­SAD.
机译:AmtR是TetR转录调节子家族的成员,是谷氨酸棒杆菌中氮控制的全球调节子。与受小分子效应子调控的其他TetR家族成员不同,AmtR受称为GlnK的蛋白质调控。已经显示,在与AmtR形成复合物之前,必须对GlnK三聚体进行腺苷化。 AmtR的生理功能已经进行了很好的研究,但是AmtR调控的转录机制的结构表征尚未完成。 AmtR已成功在空间群P21212中结晶,其中六个分子位于不对称单位中,单位细胞参数a = 153.34,b = 163.10,c = 51.93。使用Se-­SAD获得了初步阶段。

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