| Project/Area Number |
15K12221
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Environmental impact assessment
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| Research Institution | Okazaki Research Facilities, National Institutes of Natural Sciences |
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Principal Investigator |
Aono Shigetoshi 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 教授 (60183729)
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| Co-Investigator(Renkei-kenkyūsha) |
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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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | センサータンパク質 / ヘム結合タンパク質 / ヘム / 銅センサータンパク質 / センサー型転写調節因子 / X線結晶構造解析 |
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| Outline of Final Research Achievements |
As a candidate of sensorprotein for heavy metal ions, preparation and structural determination were tried with copper sensor proteins that act as acopper-sensing transcriptional regulators. And heme transport proteins in Corynebacteria were also chosen as research targets. In this work, we have studied the structural and functional relationships of HtaA and HtaB from Corynebacterium glutamicum. We determined the crystal structure of the N-, and C-terminal domains of HtaA (HtaA-N and HtaA-C, respectively) and HtaB. HtaA-N consists of 11 β strands and two short α helices and accommodates one heme molecule with Tyr58 located in the first α helix as the heme axial ligand. Tyr58 forms a hydrogen bond with His111.
HtaA-C and HtaB show similar global structures to HtaA-N. The key residues for heme-binding and recognition including the axial ligand of heme and residues involved in the hydrogen bonding interactions with heme are conserved among HtaA-N, HtaA-C, and HtaB.
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