The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer
The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer
复制标题
单对荧光共振能量转移揭示旋转F1-ATP酶的ATP等待构象
DOI：
--
复制
发表时间：
2003
影响因子：
11.1
通讯作者：
K. Kinosita
中科院分区：
文献类型：
--
作者：
R. Yasuda;T. Masaike;K. Adachi;H. Noji;H. Itoh;K. Kinosita
F1-γ酶是一种由三磷酸腺苷驱动的旋转马达，其中棒状的α亚基在由β3亚基组成的圆柱体内旋转。为了阐明旋转F1的构象，我们测量了单个F1分子中三个βS之一上的供体和γ上的受体之间的荧光共振能量转移(FRET)。FRET的产量在低浓度时呈阶梯式变化，反映了γ的阶梯式旋转。在等待状态下，FRET的产生表明线粒体F1晶体结构中的γ位置与线粒体F1晶体结构中的≈位置成逆时针方向40°(=旋转方向)，这表明在产物释放之前，晶体结构模拟亚稳态。
F1-ATPase is an ATP-driven rotary motor in which a rod-shaped γ subunit rotates inside a cylinder made of α3β3 subunits. To elucidate the conformations of rotating F1, we measured fluorescence resonance energy transfer (FRET) between a donor on one of the three βs and an acceptor on γ in single F1 molecules. The yield of FRET changed stepwise at low ATP concentrations, reflecting the stepwise rotation of γ. In the ATP-waiting state, the FRET yields indicated a γ position ≈40° counterclockwise (= direction of rotation) from that in the crystal structures of mitochondrial F1, suggesting that the crystal structures mimic a metastable state before product release.
DOI：
10.1073/pnas.92.24.10964
发表时间：
1995-11-21
影响因子：
11.1
作者：
DUNCAN, TM;BULYGIN, VV;CROSS, RL
通讯作者：
CROSS, RL