首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12.
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Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12.

机译:TyrR转录因子N末端结构域的晶体结构,负责大肠杆菌K12中芳香族氨基酸生物合成和运输的基因调控。

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摘要

The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of approximately 50 degrees . The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors.
机译:TyrR的N末端结构域的X射线结构已解析为2.3 A的分辨率。它揭示了包含ACT域,连接螺旋,PAS域和C末端螺旋的模块蛋白。不对称单元中存在两个二聚体,每对中的一个单体表现出较大的刚性运动,从而导致围绕残基74的铰接大约为50度。参考其他转录调节蛋白来讨论二聚体的结构。确定了芳香族氨基酸辅因子的推定结合位点。

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