The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
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DOI：
10.1038/nsmb1017
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发表时间：
2005-12-01
影响因子：
16.8
通讯作者：
Reinisch, KM
中科院分区：
文献类型：
--
作者：
Dong, G;Hutagalung, AH;Reinisch, KM
外囊是一个大的复合体，在所有真核生物的外囊途径的最后阶段，它是束缚囊泡所必需的。在这里，我们提出了这个复杂的exo 70 p亚基和exo 84 p的C-末端结构域的结构，分别在2.0埃和2.85埃的分辨率。Exo 70 p形成了一个160埃长的棒，具有由连续的α螺旋束组成的新折叠。Exo 84 p C末端还形成长杆（80埃），其出乎意料地具有与Exo 70 p N末端相同的折叠。我们的结构结果和我们的实验观察Exo 70 p和其他外囊亚基或Rho 3 p GTdR之间的相互作用是一致的架构，其中外囊亚基组成的大部分螺旋模块串成长杆。
The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-angstrom and 2.85-angstrom resolution, respectively. Exo70p forms a 160-angstrom-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 angstrom), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.