| Budget Amount *help |
¥19,890,000 (Direct Cost: ¥15,300,000、Indirect Cost: ¥4,590,000)
Fiscal Year 2014: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2013: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2012: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
|
|---|
| Outline of Final Research Achievements |
P-type ATPases possess common domain-structure and couple the ATP hydrolysis with the specific cation-transport. In this study, we first revealed by extensive mutations and kinetic analyses of Ca-ATPase that the second transmembrane helix plays critical roles via its motions and changes in its secondary structure for transferring the motions of cytoplasmic domains to the transmembrane cation transport sites there by for the energy coupling. We also revealed that unique structural fluctuation is equipped in each of the phosphoenzyme intermediates, and the fluctuation functions to accomplish the proper forward transport reaction. Thus we contributed to the comprehensive understanding of the P-type ATPase mechanism and an establishment of molecular basis for diseases developed by the pump defects.
|
