Linkage between Isomerization of Phosphoenzyme Intermediate and Calcium Transport in Sarcoplasmic Reticulum Calcium Pump
Project/Area Number |
20570102
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
|
Research Institution | Asahikawa Medical College |
Principal Investigator |
DAIHO Takashi Asahikawa Medical College, 医学部, 准教授 (90207267)
|
Project Period (FY) |
2008 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | Ca<^2+>-ATPase / カルシウムポンプ / イオン輸送 / 酵素反応速度論 / 部位特異的変異 / P-type ATPase / 中間体構造アナログ / 小胞体 / Ca^<2+>-ATPase / P-tvpe ATPase / mutation / sarco(endo)plasmic reticulum / analog / phosphoenzyme / calcium / ion transport / Ca^<2+> / Mn^<2+>-ATPase / Golei annaratus / keratinocyte / P-tvoe ATPase |
Research Abstract |
Ca^<2+> is transported by sarcoplasmic reticulm Ca^<2+>-pump through formation and hydrolysis of phosphoenzyme intermediate (EP) phosphorylated with ATP. Ca^<2+> ions bound to EP from cytoplasm are released into lumen in its isomerization (E1P・Ca_2→E2P). I found structural elements essential for the isomerization, and found a new EP intermediate (E2P・Ca_2) between these two EPs. To perform atomic or other structural analysis, I then developed stable analogs for E1P・Ca_2 and E2P・Ca_2. Furthermore, I have elucidated some new roles of the K+ ion bound to EP during Ca^<2+> transport and the mechanism of pump activation by high-concentration of ATP.
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Report
(4 results)
Research Products
(52 results)