Structure-function studies of B12-containing photosensor proteins
| Project/Area Number |
26840027
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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 | Institute for Molecular Science |
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Principal Investigator |
Muraki Norifumi 分子科学研究所, 生命・錯体分子科学研究領域, 助教 (20723828)
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| Research Collaborator |
Aono Shigetoshi
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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 |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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| Keywords | X線結晶解析 / 光センサー / 光受容体 / 結晶構造解析 / ビタミンB12 / 転写因子 / 結晶構造解析法 / センサータンパク質 / 光応答 |
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| Outline of Final Research Achievements |
Recently, a novel transcription regulator CarH has been characterized as a cobalamin-dependent photosensor. Though it is reported that CarH regulates the biosynthesis of carotenoids in response to light, the detail molecular mechanisms of light sensing and functional regulation of CarH in response to light were unclear.
We determined the crystal structure of adenosylcobalamin-bound CarH from Thermus thermophilus.
CarH consists of the N-terminal DNA binding domain and the C-terminal sensor domain. The adenosyl group of adenosylcobalamin stabilizes the conformation of the sensor domain. We assumed that loss of adenosyl group upon photosensing results in change of the quaternary structure from tetramer to monomer.
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Report
(4 results)
Research Products
(16 results)
