Structural analysis of rice granule-bound starch synthase
| Project/Area Number |
26440038
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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 | National Agriculture and Food Research Organization (2016)
National Institute of Agrobiological Sciences (2014-2015) |
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Principal Investigator |
Fujimoto Zui 国立研究開発法人農業・食品産業技術総合研究機構, 高度解析センター, 上級研究員 (20370679)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | イネ / 顆粒結合型デンプン合成酵素 / アミロース / Ｘ線結晶構造解析 / X線結晶構造解析 / 糖鎖結合複合体 |
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| Outline of Final Research Achievements |
Granule-bound starch synthase I(GBSSI) catalyze the amylose (α-1,4-linked glucose chain ) elongation process by adding glucose from nucleotide diphosphate glucose. We conducted the structural analysis of rice GBSSI in complex with maltooligosaccharides having the α-1,4-linked glucose moieties to clarify the substrate-recognition mechanism of the plant enzyme. The structures had two Rossmann fold N- and C-domains, connected by the canonical two hinge peptides, and an interdomain disulfide bond that appears to be conserved in the Poaceae plant family. The catalytic site appeared to be located in the concave of two domains, and the flexible loop regions near the catalytic concave appeared to be the carbohydrate-binding site.
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Report
(4 results)
Research Products
(1 results)
