首页> 外文期刊>Journal of Molecular Biology >Crystal structures of the multidrug binding repressor Corynebacteriumglutamicum CgmR in complex with inducers and with an operator.
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Crystal structures of the multidrug binding repressor Corynebacteriumglutamicum CgmR in complex with inducers and with an operator.

机译:多药结合阻遏物谷氨酸棒杆菌CgmR的晶体结构与诱导剂和操纵子复合。

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摘要

CgmR (CGL2612) from Corynebacterium glutamicum is a multidrug-resistance-related transcription factor belonging to the TetR family, which is a protein family of widespread bacterial transcription factors typically involved in environmental response. Here, we report the crystal structures of CgmR homodimeric repressor in complex with two distinct inducers (1.95 and 1.4 A resolution) and with an operator (2.5 A resolution). The CgmR-operator complex showed that two CgmR dimers bound to the operator, and each half-site of the palindromic operator was asymmetrically recognized by two DNA-binding domains from different dimers on the opposite sides of the DNA. The inducer complexes demonstrated that both bound inducers act as a wedge to alter the operator-binding conformation of the repressor by steric inhibition. As steric hindrance is used, various drugs should act as inducers if they have sufficient volume for the conformation change and if their bindings sufficiently reduce free energy. The comparative structural study of CgmR free protein, in complex with operator, and with inducers, implies the other mechanism that might contribute to multidrug response of the repressor.
机译:谷氨酸棒杆菌的CgmR(CGL2612)是属于TetR家族的与多药耐药相关的转录因子,TetR家族是通常参与环境响应的广泛细菌转录因子的蛋白家族。在这里,我们报告CgmR同源二聚体阻遏物的晶体结构与两个不同的诱导剂(1.95和1.4 A分辨率)和一个算子(2.5 A分辨率)复合。 CgmR-操纵子复合物显示两个CgmR二聚体与操纵子结合,回文操纵子的每个半位点被来自DNA相对侧的不同二聚体的两个DNA结合域非对称地识别。诱导物复合物表明,两个结合的诱导物均起楔形作用,以通过空间抑制改变阻遏物的操纵子结合构象。由于使用了空间位阻,如果各种药物具有足以改变构象的体积,并且其结合充分降低了自由能,则它们应充当诱导剂。对CgmR游离蛋白的比较结构研究,与操纵基因和诱导物复合,暗示了可能有助于阻遏物多药反应的其他机制。

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