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

2015 Fiscal Year Final Research Report

• 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
• Keywords: 膜タンパク質 / 結晶構造解析 / 細菌 / 抗菌 / 多剤耐性

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.

Free Research Field

構造生命化学