Cell wall peptidoglycan recognition/hydrolysis mechanisms of Clostridium perfringens lytic enzymes based on X-ray structures
| Project/Area Number |
15K06973
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kagawa University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
吉田 裕美 香川大学, 総合生命科学研究センター, 准教授 (10313305)
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| Co-Investigator(Renkei-kenkyūsha) |
TAMAI Eiji 松山大学, 薬学部, 准教授 (40333512)
NOGUCHI Keiichi 東京農工大学, 学術研究支援総合センター, 准教授 (00251588)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | X線結晶構造解析 / 溶菌酵素 / グリコシドヒドロラーゼ / 細菌細胞壁 / ペプチドグリカン / ウェルシュ菌 / X線結晶解析 / SH3ドメイン / 糖鎖加水分解酵素 / ソーテース / グルコサミニダーゼ / ディフィシル菌 |
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| Outline of Final Research Achievements |
Gram-positive bacteria possess a thick cell wall that surrounds their cytoplasmic membranes and provides physical protection. The bacterial cell wall is a mesh polymer of peptidoglycans, in which linear glycan backbones are cross-linked by species-specific peptide side chains. Autolysins can partially hydrolyze cell wall peptidoglycan into small sections to regulate cell separation/division and the growth-phase of bacteria. An X-ray structure of Clostridium perfringens autolysin catalytic domain was determined, giving new insights into the catalytic reaction mechanism for the hydrolysis of cell wall peptidoglycan. The pathogenesis and infectivity of Gram-positive bacteria are mediated by many surface proteins that are covalently attached to peptidoglycans of the cell wall. The covalent attachment of these proteins is catalyzed by sortases. X-ray structures of Clostridium perfringens sortase B and its inactive mutant form were determined.
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Report
(4 results)
Research Products
(10 results)
