Structure of the Ca2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-A resolution.
Structure of the Ca2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-A resolution.
复制标题
肌浆网 Ca2 泵的结构：沿脂质双层的 9-A 分辨率视图。
DOI：
10.1016/s0006-3495(98)77493-4
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Toyoshima,C
中科院分区：
文献类型：
--
作者：
Ogawa,H;Stokes,DL;Sasabe,H;Toyoshima,C
我们已经使用来自肌浆网的ATP驱动的钙泵的多层晶体来解决钙结合到酶的结构效应。它们是一堆堆圆盘状的二维晶体。通过冷冻水化电子显微镜以9- 10分辨率获得沿脂质双层沿着投影的密度图。虽然只是在投影，更多的结构细节揭示比以前可用的，特别是在跨膜区。定量比较与模型获得的管状晶体中形成的这种酶在没有钙。出乎意料的大差异构象被发现，特别是在胞质结构域。
We have used multilamellar crystals of the ATP-driven calcium pump from sarcoplasmic reticulum to address the structural effects of calcium binding to the enzyme. They are stacks of disk-shaped two-dimensional crystals. A density map projected along the lipid bilayer was obtained at 9-Å resolution by frozen-hydrated electron microscopy. Although only in projection, much more details of the structure were revealed than previously available, especially in the transmembrane region. Quantitative comparison was made with the model obtained from the tubular crystals of this enzyme formed in the absence of calcium. Unexpectedly large differences in conformation were found, particularly in the cytoplasmic domain.