Molecular mechanism of the construction of the bacterial flagellar rod.
| Project/Area Number |
20370036
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
IMADA Katsumi Osaka University, 大学院・理学研究科, 教授 (40346143)
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| Co-Investigator(Renkei-kenkyūsha) |
MINAMINO Tohru 大阪大学, 大学院・生命機能研究科, 准教授 (20402993)
KATO Takayuki 大阪大学, 大学院・生命機能研究科, 助教 (20423155)
NAMBA Keiichi 大阪大学, 大学院・生命機能研究科, 教授 (30346142)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥19,370,000 (Direct Cost: ¥14,900,000、Indirect Cost: ¥4,470,000)
Fiscal Year 2010: ¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2009: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
Fiscal Year 2008: ¥6,760,000 (Direct Cost: ¥5,200,000、Indirect Cost: ¥1,560,000)
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| Keywords | X線結晶解析 / 分子機械 / ナノマシン / 生物物理 / 蛋白質 / 生体分子 |
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| Research Abstract |
In this study, we determined the crystal structure of a C-terminal fragment of FlgJ, which has a muramidase activity, and revealed the molecular mechanism of the peptidoglican hydrolysis. The active site structure and the overall folding of FlgJ resemble those of hen egg white lysozyme. Interestingly, the activity of FlgJ is strongly inhibited by a very small amount of cation. We reconstituted distal rod by adding rod proteins to the purified flagellar hook. Moreover, we elucidated the interaction between the rod and FlgD, the hook cap protein.
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Report
(4 results)
Research Products
(43 results)
