| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Outline of Final Research Achievements |
Enterococcus hirae V-ATPase is an ion-transporting rotary enzyme that consists of nine kinds of subunits. In order to understand the molecular mechanism of this enzyme, it is essential to clarify the overall architecture and the interaction among these subunits. In this study, we succeeded in X-ray crystal structure analysis of the catalytic headpiece (V1-ATPase) and present ATP-hydrolytic rotatory mechanism of V1-ATPase. Furthermore, based on biochemical and surface plasmon resonance analyses on reconstitution of V1-ATPase complex and mutagenesis of V0 rotor ring subunit, the features of interaction among rotor and stator subunits of V-ATPase were revealed.
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