Mohraz M, Simpson M V, Smith P R
J Cell Biol. 1987 Jul;105(1):1-8. doi: 10.1083/jcb.105.1.1.
The structure of Na,K-ATPase has been studied by electron microscopy and image reconstruction. A three-dimensional structure of this enzyme has been obtained to an overall resolution of 2.5 nm using data from specimens of negatively stained dimer sheets tilted through a range of angles +/- 60 degrees. The reconstruction shows a complex mass distribution consisting of ribbons of paired molecules extending approximately 6.0 nm from the cytoplasmic side of the membrane. The molecular envelope consists of a massive "body" with "lobe" and "arm" structures projecting from it. The body has a columnar shape and is tilted with respect to the plane of the membrane. The region of interaction responsible for dimer formation is located between two bodies and is clearly visible in the reconstruction. It has been identified as a segment in the amino-terminal portion of the alpha subunit. The arms that interconnect the ribbons are located close to the membrane and are most probably formed by the beta subunits.
钠钾-ATP酶的结构已通过电子显微镜和图像重建技术进行了研究。利用负染二聚体片标本在±60度范围内倾斜的一系列角度的数据,已获得该酶的三维结构,整体分辨率达到2.5纳米。重建结果显示出一种复杂的质量分布,由成对分子的条带组成,从膜的细胞质侧延伸约6.0纳米。分子包膜由一个巨大的“主体”组成,“叶”和“臂”结构从主体伸出。主体呈柱状,相对于膜平面倾斜。负责二聚体形成的相互作用区域位于两个主体之间,在重建中清晰可见。它已被确定为α亚基氨基末端部分的一个片段。连接条带的臂靠近膜,很可能由β亚基形成。