Crystal structure of the mouse endonuclease G
作者: Kwang-Hyun ParkSei Mee YoonHyung Nam SongJoon-Hyuck YangSeong Eon RyuEui-Jeon Woo
作者单位: 1Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon, 305-806, Republic of Korea
2Department of Proteome Structural Biology, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon, 305-333, Republic of Korea
3Department of Bioengineering, College of Engineering, Hanyang University, Seoul, 04673, Republic of Korea
4Department of Health Informatics and Management, College of Medicine, Chungbuk National University, Cheongju, Republic of Korea
刊名: Biochemical and Biophysical Research Communications, 2020
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2020.03.060
关键词: ApoptosisCrystal structureEndoGEndonucleaseEndoG inhibitors
英文摘要: Abstract(#br)Endonuclease G (EndoG) is a mitochondrial enzyme that responds to apoptotic stimuli by translocating to the nucleus and cleaving the chromatin DNA. The molecular mechanism of EndoG still remains unknown in higher organisms. Here, we determined the crystal structure of mouse EndoG at ∼1.96 Å resolution. The EndoG shows an altered dimeric configuration in which N-terminal region of one subunit interact to the other subunit in dimer. The deletion of this region that is highly conserved in mammalian EndoGs resulted in a monomer with significantly reduced activity suggesting the association of the dimeric arrangement into the nuclease activity. Furthermore, we observed a large conformational change in the loop of the active site groove in EndoG, which corresponds to the DNA...
全文获取路径: Elsevier  (合作)

  • endonuclease 核酸内切酶
  • mouse 小鼠
  • structure 构造