The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles
The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles
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DOI：
10.1006/jsbi.2001.4395
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发表时间：
2001-07-01
影响因子：
3
通讯作者：
Grüber, G
中科院分区：
文献类型：
--
作者：
Radermacher, M;Ruiz, T;Grüber, G
我们测定了烟草天蛾V-1-ATP酶的结构，分辨率为1.8 nm，这是第一次揭示了该酶的内部特征。V-1-ATP酶由一个直径为13.5 nm的头片段和一个连接V-1和膜结合区V-O的6 nm长柄组成，头片段由6个大小大致相等的细长亚基A（3）和B-3组成。在分子的中心是一个贯穿A（3）B（3）六聚体长度的空腔。在空腔内，可以看到中央茎仅与两个催化A亚基连接。该结构通过随机圆锥重建技术和角度细化的组合获得。其他最近开发的技术，包括同步平移旋转对齐的0度图像，倾斜图像的对比度传递函数校正的方法，和两步氡反演算法。(C)北京：科学出版社.
We determined the structure of the V-1-ATPase from Manduca sexta to a resolution of 1.8 nm, which for the first time reveals internal features of the enzyme. The V-1-ATPase consists of a headpiece of 13.5 nm in diameter, with six elongated subunits, A(3) and B-3, of approximately equal size, and a stalk of 6 nm in length that connects V-1 with the membrane-bound domain, V-O. At the center of the molecule is a cavity that extends throughout the length of the A(3)B(3) hexamer. Inside the cavity the central stalk can be seen connected to only two of the catalytic A subunits. The structure was obtained by a combination of the Random Conical Reconstruction Technique and angular refinements. Additional recently developed techniques that were used include methods for simultaneous translational rotational alignment of the 0 degrees images, contrast transfer function correction for tilt images, and the Two-Step Radon Inversion Algorithm. (C) 2001 Academic Press.