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谷氨酸棒杆菌全局氮调节因子AmtR的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of the global nitrogen regulator AmtR from Corynebacterium glutamicum.

作者信息

Hasselt Kristin, Sevvana Madhumati, Burkovski Andreas, Muller Yves A

机构信息

Lehrstuhl für Mikrobiologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Germany.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1123-7. doi: 10.1107/S174430910903663X. Epub 2009 Oct 30.

Abstract

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 P2(1)2(1)2, with six molecules in the asymmetric unit and unit-cell parameters a = 153.34, b = 163.10, c = 51.93 angstrom . Preliminary phases were obtained using Se-SAD.

摘要

AmtR是转录调节因子TetR家族的成员,是谷氨酸棒杆菌氮控制的全局调节因子。与其他受小分子效应物调节的TetR家族成员不同,AmtR受一种名为GlnK的蛋白质调节。研究表明,GlnK三聚体在与AmtR形成复合物之前必须进行腺苷酸化。AmtR的生理功能已得到很好的研究,但对AmtR调节转录的机制方面的结构表征尚未完成。AmtR已成功在空间群P2(1)2(1)2中结晶,不对称单元中有六个分子,晶胞参数a = 153.34,b = 163.10,c = 51.93埃。使用硒单波长反常散射法获得了初步相位。

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