A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein
| Project/Area Number |
22550153
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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 |
Chemistry related to living body
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| Research Institution | Hiroshima University |
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Principal Investigator |
SUGIYAMA Masanori 広島大学, 大学院・医歯薬保健学研究院, 教授 (30106801)
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| Co-Investigator(Kenkyū-buntansha) |
MATOBA Yasuyuki 広島大学, 大学院・医歯薬保健学研究院, 准教授 (90363051)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2012: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | チロシナーゼ / X 線結晶構造解析 / 銅イオン / 金属シャペロン / メラニン生成酵素 / 放線菌 / タンパク質 / ラマンスペクトル / 吸収スペクトル / X線結晶構造解析 |
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| Research Abstract |
The Cu(II)-soaked crystal structure of tyrosinase in a complex with a protein, designated “caddie”, which has previously determined by us, displays to possess two copper ions at the catalytic center. We observed two copper-binding sites in the caddie protein, speculating that the copper bound to caddie may be transported to the tyrosinase catalytic center. In the present study, at the 1.16 to 1.58 A resolution, we determined the crystal structures of tyrosinase complexed with a caddie prepared by altering the soaking time of the copper ion and the structures of tyrosinase complexed with a few mutants of a caddie which displays no or little ability to activate tyrosinase. Based on these structures, we propose a molecular mechanism to transport two copper ions to the tyrosinase catalytic center, which is assisted by a caddie as a metallochaperone.
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Report
(4 results)
Research Products
(19 results)
