Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII
对金黄色葡萄球菌RNase HII新型功能二聚体的结构见解
作者: Tianrong HangXiaozhen ZhangMinhao WuChengliang WangShenglong LingLing XuQingguo GongChanglin TianXuan ZhangJianye Zang
作者单位: 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Jinzhai Road, Hefei, 230026, China
2Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, 230027, China
刊名: Biochemical and Biophysical Research Communications, 2018, Vol.503 (3), pp.1207-1213
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2018.07.026
关键词: DNA repairRNase HIIDimerizationEnzyme catalysisProtein-nucleic acid interactionX-ray crystallography
英文摘要: Abstract(#br)RNase HII exists ubiquitously in organisms and functions as a monomer in prokaryotes. We determined the crystal structure of Staphylococcus aureus RNase HII (Sa-RNase HII), which displays a novel dimer conformation, with the active site of each monomer covered by the other one. Both small-angle X-ray scattering and gel-filtration analysis confirmed that Sa-RNase HII exists as a homodimer in solution. Enzymatic analysis revealed that the “self-inhibited” dimeric form is catalytically active. Furthermore, continuous-wave electron paramagnetic resonance experiments clarified that the Sa-RNase HII dimer undergoes a large conformational change upon substrate binding, but remains a dimer to catalyze the reaction. Our structural and biochemical studies identified a novel functional...
全文获取路径: Elsevier  (合作)

  • novel 长篇小说
  • dimer 二聚物
  • functional 功能的
  • RNase 核糖核酸酶