Molecular structure and flexibility of the yeast coatomer as revealed by electron microscopy.
Molecular structure and flexibility of the yeast coatomer as revealed by electron microscopy.
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DOI：
10.1016/j.jmb.2011.03.029
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发表时间：
2011-05-20
影响因子：
5.6
通讯作者：
Walz T
中科院分区：
文献类型：
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作者：
Yip CK;Walz T
外壳蛋白复合体I(COPI)是细胞内三种主要的囊泡载体之一，介导了早期的分泌途径和从高尔基体到内质网的逆行运输。CopI囊泡是通过激活供体膜上调节的GTP酶Arf1和随后招募Coom er来产生的，Coom er是一种由七个稳定相关成分组成的外壳蛋白复合体。Coomer的功能是结合和隔离货物分子，并组装成一个包围COPI囊泡表面的聚合蛋白外壳。人们对这种七聚体复合体的结构性质知之甚少。我们分离了天然酵母辅酶，并用单粒子电子显微镜(EM)检测了其结构和亚基组成。我们的分析提供了第一张完整的辅酶的三维图像，并揭示了相当大的构象灵活性可能是其支架功能的关键。
Coat protein complex I (COPI) coated vesicles, one of three major types of vesicular carriers in the cell, mediate the early secretory pathway and retrograde transport from the Golgi to the endoplasmic reticulum. COPI vesicles are generated through activation of the regulatory GTPase Arf1 at the donor membrane and the subsequent recruitment of coatomer, a coat protein complex consisting of seven stably associated components. Coatomer functions in binding and sequestering cargo molecules and assembles into a polymeric protein shell that encompasses the surface of COPI vesicles. Little is known about the structural properties of this heptameric complex. We have isolated native yeast coatomer and examined its structure and subunit organization by single-particle electron microscopy (EM). Our analyses provide the first three-dimensional picture of the complete coatomer, and reveal substantial conformational flexibility likely to be critical for its scaffolding function.
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影响因子：
5.6
作者：
Yu, Wenyu;Lin, Jian;Xia, Bin
通讯作者：
Xia, Bin
影响因子：
64.8
作者：
Stagg, SM;Gürkan, C;Balch, WE
通讯作者：
Balch, WE
DOI：
10.1002/jemt.1060090405
发表时间：
1988-08-01
期刊：
JOURNAL OF ELECTRON MICROSCOPY TECHNIQUE
影响因子：
--
作者：
RADERMACHER, M
通讯作者：
RADERMACHER, M
影响因子：
4.8
作者：
Zhao, LY;Helms, JB;Wieland, FT
通讯作者：
Wieland, FT
COG囊泡束缚复合物的分子组织。
影响因子：
16.8
作者：
通讯作者：
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