New kinase regulation mechanism found in HipBA: a bacterial persistence switch
New kinase regulation mechanism found in HipBA: a bacterial persistence switch
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DOI：
10.1107/s0907444909018800
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发表时间：
2009-08-01
期刊：
影响因子：
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通讯作者：
Fisher, Douglas A.
中科院分区：
文献类型：
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作者：
Evdokimov, Artem;Voznesensky, Igor;Fisher, Douglas A.
细菌持久性是指单个细胞随机进入一段休眠期的能力，在此期间，细胞受到抗生素的保护。在大肠杆菌中，持久性由蛋白激酶HipA及其dna结合伙伴hib的活性调节，hib是HipA活性和hip操纵子转录的强抑制剂。通过将SAD技术应用于汞衍生物，求解了HipBA配合物的晶体结构。本文讨论了汞浸泡对天然HipA晶体的偶然和有趣的影响，以及在HipA表面发现的有趣的色氨酸结合袋。我们还提出了一个与现有结构和生化数据一致的hipa调控模型。
Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.