Low resolution structure of subunit b (b22–156) of Escherichia coli F1FO ATP synthase in solution and the b−δ assembly
Low resolution structure of subunit b (b22–156) of Escherichia coli F1FO ATP synthase in solution and the b−δ assembly
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DOI：
10.1007/s10863-008-9154-x
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发表时间：
2008-07
影响因子：
3
通讯作者：
R. Priya;V. S. Tadwal;M. Roessle;S. Gayen;C. Hunke;Weng Chuan Peng;J. Torres;G. Grüber
中科院分区：
文献类型：
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作者：
R. Priya;V. S. Tadwal;M. Roessle;S. Gayen;C. Hunke;Weng Chuan Peng;J. Torres;G. Grüber
大肠杆菌F1FOATP合酶亚基b(b22-156)可溶性结构域的第一个低分辨率溶液结构是根据小角X射线散射数据确定的。二聚体蛋白具有类似回旋镖的形状，总长度为16.2±0.3 nm。荧光相关光谱 (FCS) 显示该蛋白质与 δ 亚基有效结合，证实了它们所描述的邻域。使用δ亚基的重组C端结构域(δ91-177)和亚基b、b120-140和b140-156的C端肽，进行FCS滴定实验以分配参与δ-b组装的片段。这些数据确定了 C 末端 tailb140-156 与 δ91-177 相互作用。该肽的新颖 3D 结构已通过 NMR 光谱确定。该分子在溶液中形成稳定的螺旋结构，并在氨基酸 140 至 145 之间具有灵活的尾部。
The first low resolution solution structure of the soluble domain of subunitb(b22–156) of theEscherichia coliF1FOATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2±0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit δ, confirming their described neighborhood. Using the recombinant C-terminal domain (δ91–177) of subunit δ and the C-terminal peptides of subunitb,b120–140andb140–156, FCS titration experiments were performed to assign the segments involved in δ−bassembly. These data identify the very C-terminal tailb140–156to interact with δ91–177. The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.