Crystal structure analysis of quorumon-receptor membrane protein complex that controls the expression of virulence factor in the pathogen

• Project/Area Number: 25292057
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Applied biochemistry
• Research Institution: The University of Tokyo
• Principal Investigator: Nagata Koji 東京大学, 農学生命科学研究科, 准教授 (30280788)
• Co-Investigator(Kenkyū-buntansha): NAKAYAMA Jiro 九州大学, 大学院農学研究院, 准教授 (40217930)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Project Status: Completed (Fiscal Year 2015)
• Budget Amount: ¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000); Fiscal Year 2015: ¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000); Fiscal Year 2014: ¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000); Fiscal Year 2013: ¥8,840,000 (Direct Cost: ¥6,800,000、Indirect Cost: ¥2,040,000)
• Keywords: 膜タンパク質 / 結晶構造解析 / 細菌 / 抗菌 / 多剤耐性 / 構造生物学 / 複合体構造 / 多剤排出輸送体

Outline of Final Research Achievements

We performed X-ray crystallographic analysis of the crystals obtained from the purified sample of FsrC that was supplemented with GBAP (an agonist) or an antagonist. The analysis revealed that the crystals obtained did not contain FsrC but instead contain AcrB, an E coli membrane protein involved in multidrug efflux. There were two kinds of AcrB; one was the crystal of the know AcrB structure, whereas the other was the crystal of a new AcrB structure. The analysis of the latter crystal structure is in progress because this crystal structure is as an important target as the FsrC structure. In addition, we found that the expression level of FsrC-GFP fusion protein was improved by coexpressing some kind of protease inhibitor.

Research Products

• [Remarks] 細胞間情報伝達に関わるタンパク質の構造・機能解析
  • URL: http://fesb.ch.a.u-tokyo.ac.jp/main.html