Structure/function relationship and cell surface localization mechanism of bacterial flagelin
Project/Area Number |
20380049
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied microbiology
|
Research Institution | Kyoto University |
Principal Investigator |
MURATA Kousaku Kyoto University, 農学研究科, 教授 (90142299)
|
Co-Investigator(Kenkyū-buntansha) |
橋本 渉 京都大学, 農学研究科 (30273519)
三上 文三 京都大学, 農学研究科 (40135611)
|
Project Period (FY) |
2008 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2010: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2009: ¥6,760,000 (Direct Cost: ¥5,200,000、Indirect Cost: ¥1,560,000)
Fiscal Year 2008: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
|
Keywords | フラジェリン / 鞭毛 / ペプチドグリカン加水分解酵素 / メタロペプチダーゼ / X線結晶構造解析 / 体腔形成細菌 / 細菌細胞表層構造 / アルギン酸 / ペプチドグリカン加水分解楮 / スフィンゴモナス属細菌 / 超チャネル / ペプチドグリカン構造 / ペプチドグリカン分解酵素 / X線結晶構造 / フラジェリン進化 |
Research Abstract |
Flagellin, a flagellar protein, in a bacterium Sphingomonas sp. A1 does not participate in the formation of flagella, localizes on the cell surface, and shows highly potent capability to bind alginate, an acidic polysaccharide present in brown sea algae. To elucidate these characteristic properties of flagellin, three-dimensional structures of flagellin, flagellin-anchoring protein on the cell surface, and peptidoglycan-hydrolyzing enzyme were determined and their relationships between structure and function clarified. Based on these results, the biological significance of flagellin were discussed from the standpoint of sensor for alginate, cell surface structure, and molecular evolution.
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Report
(4 results)
Research Products
(42 results)