structural basis of the decamer architecture of a higher plant glutamine synthetase and substrate recognition mechanism
| Project/Area Number |
21570111
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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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 | University of Yamanashi |
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Principal Investigator |
KUSUNOKI Masami 山梨大学, 大学院・医学工学総合研究部, 教授 (90135749)
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| Co-Investigator(Renkei-kenkyūsha) |
HASE Toshiharu 大阪大学, たんぱく質研究所, 教授 (00127276)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2009: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 窒素同化 / 構造生物学 / 結晶構造 / グルタミン合成酵素 / 植物生理 / X線 / 酵素反応 / 活性部位 / 植物整理 / 触媒 / 結晶 / 立体構造 / 窒素代謝 / 植物生理学 / グルタミン合成酵 |
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| Research Abstract |
We studied GS1a isoenzyme of maize glutamine synthetase in this research. Residues around Phe150 are responsible for interactions between two pentamers and we prepared many alanine-mutant enzymes for these residues. As a result we found the alanine mutants with high Km values for residues at the location spanning the two-pentamer interaction region and the substrate glutamic acid entry region into the catalytic site. The former region is distant from the catalytic site and we obtained two good crystals of G241A and W243A mutant enzymes at 2. 10 A and 2. 80 A resolutions, respectively there. These crystal structures revealed that there is a region on the enzyme involved in the substrate affinity distinct from the catalytic site.
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Report
(4 results)
Research Products
(15 results)
