Evdokimov Artem, Voznesensky Igor, Fennell Kimberly, Anderson Marie, Smith James F, Fisher Douglas A
Pfizer Inc, Groton, Connecticut, USA.
Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):875-9. doi: 10.1107/S0907444909018800. Epub 2009 Jul 17.
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.
细菌持留性是指单个细胞随机进入休眠期的能力，在此期间细胞对抗生素具有抗性。在大肠杆菌中，持留性受蛋白激酶HipA及其DNA结合伴侣HipB的活性调控，HipB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，解析了HipBA复合物的晶体结构。本文讨论了汞浸泡对天然HipBA晶体产生的偶然且有趣的影响，以及在HipA表面发现的有趣的色氨酸结合口袋。还提出了一个与现有结构和生化数据一致的HipA调控模型。
