| Project/Area Number |
16K18498
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
Kato Koji 北海道大学, 先端生命科学研究院, 助教 (30452428)
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| Research Collaborator |
SAKURAI Naofumi
SUZUKI Wakana
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | tRNAスプライシング / X線結晶構造解析 / tRNスプライシング / tRNA Spricing / 蛋白質－RNA複合体 / 分子生物学 / X線結晶解析 / 核酸－タンパク質複合体 / 蛋白質 / tRNA |
|---|
| Outline of Final Research Achievements |
Crystal structure of Trl1 ligase domain (Trl1-LD) - GMP complex was determined with 2.75 angstrom resolution. Two molecules of GMP were stacked and bonded near the active center of Trl1-LD. As a result of detailed analysis of the complex structure, basic amino acids were concentrated around two molecules of GMPs. From these facts, it was considered that these GMPs are mimicking tRNA exons in the ligation process. Based on this structure, it was possible to infer the binding mode of tRNA of Trl1-LD.
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