肌浆网Ca2+泵的结构：以9埃分辨率沿脂质双层观察。
Structure of the Ca2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-A resolution.
作者信息
Ogawa H, Stokes D L, Sasabe H, Toyoshima C
机构信息
Institute of Molecular and Cellular Biosciences, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan.
出版信息
Biophys J. 1998 Jul;75(1):41-52. doi: 10.1016/S0006-3495(98)77493-4.
Abstract
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-A 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.
摘要
我们利用来自肌浆网的ATP驱动钙泵的多层晶体来研究钙与该酶结合的结构效应。它们是盘状二维晶体的堆叠。通过冷冻水合电子显微镜在9埃分辨率下获得了沿脂质双层投影的密度图。尽管只是投影图，但揭示出的结构细节比以前更多，特别是在跨膜区域。与在无钙条件下形成的该酶管状晶体所获得的模型进行了定量比较。结果发现构象存在意想不到的巨大差异，尤其是在细胞质结构域。
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