Kumarevel Thirumananseri, Tanaka Tomoyuki, Nishio Megumi, Gopinath Subash C B, Takio Koji, Shinkai Akeo, Kumar Penmetcha K R, Yokoyama Shigeyuki
RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
J Struct Biol. 2008 Jan;161(1):9-17. doi: 10.1016/j.jsb.2007.08.017. Epub 2007 Sep 8.
The emergence of bacterial resistance to multiple drugs poses a serious and growing health concern. Understanding and deciphering the mechanisms of these multiple drug resistance regulatory proteins through structural or biochemical means is an important endeavor. Here, we present the crystal structure of ST1710 from Sulfolobus tokodaii strain 7 in two different crystal forms, at 1.80 and 2.0A, respectively. The overall structure of the ST1710 dimer shares the topology of the MarR family of proteins, with each subunit containing a winged helix-turn-helix DNA-binding motif. We also show the protein-DNA interactions by biochemical methods. Our molecular modeling analysis suggested that Asp88 and Arg90 are the key residues in ST1710 involved in the protein-DNA interactions.
细菌对多种药物产生耐药性的现象日益严重，对健康构成了重大且不断加剧的威胁。通过结构或生化手段来理解和解析这些多重耐药调控蛋白的机制是一项重要工作。在此，我们展示了来自嗜热栖热菌7号菌株的ST1710以两种不同晶体形式的晶体结构，分辨率分别为1.80埃和2.0埃。ST1710二聚体的整体结构具有MarR家族蛋白的拓扑结构，每个亚基包含一个带翼的螺旋-转角-螺旋DNA结合基序。我们还通过生化方法展示了蛋白质与DNA的相互作用。我们的分子模拟分析表明，Asp88和Arg90是ST1710中参与蛋白质与DNA相互作用的关键残基。
