Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding
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DOI：
10.1111/j.1365-2958.2009.06753.x
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发表时间：
2009-07-01
影响因子：
3.6
通讯作者：
Latour, J. -M.
中科院分区：
文献类型：
--
作者：
Jacquamet, L.;Traore, D. A. K.;Latour, J. -M.
在枯草芽孢杆菌中，转录因子PerR是一种铁依赖的H2 O2传感器。传感机制依赖于调节位点的两个组氨酸残基的选择性金属催化氧化。在这里，我们提出的第一个晶体结构的活性PerR蛋白质与Mn 2+离子的复合物。此外，进行X射线吸收光谱实验以表征蛋白质的相应铁形式。这两项研究揭示了一个五坐标安排的监管网站，涉及三个组氨酸和两个组氨酸。其中一个组氨酸配体属于N-末端结构域。该残基与调节金属的结合允许蛋白质采用适合于DNA结合的卡尺样构象。由于该组氨酸在所有PerR和绝大多数Fur蛋白中是保守的，因此很可能由调节金属诱导的变构开关对于该金属调节剂家族是普遍的。
P>In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H2O2. The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn2+ ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta-coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.