Crystal structure of the S-cerevisiae exocyst component Exo70p
Crystal structure of the S-cerevisiae exocyst component Exo70p
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DOI：
10.1016/j.jmb.2005.09.099
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发表时间：
2006-02-10
影响因子：
5.6
通讯作者：
Weis, WI
中科院分区：
文献类型：
--
作者：
Hamburger, ZA;Hamburger, AE;Weis, WI
外囊是一种进化上保守的多蛋白复合物，是高尔基体后囊泡靶向和对接质膜所需的。通过与多种蛋白质（包括小 GTP 酶）的相互作用，外囊被认为可以整合来自细胞的信号，并发出到达质膜的囊泡已准备好融合的信号。在这里，我们以 3.5 埃的分辨率描述了来自酿酒酵母的外囊成分之一 Exo70p 的三维晶体结构。 Exo70p 以 GTP 依赖性方式结合小 GTP 酶 Rho3p，平衡解离常数约为 70 μM。Exo70p 是长度约为 155 A 的延伸杆，主要由 α 螺旋组成，并且是一种新型折叠。该结构提供了 Exo70 蛋白家族的第一个视图，并提供了研究该外囊成分的分子功能的框架。 (c) 2005 Elsevier Ltd. 保留所有权利。
The exocyst is an evolutionarily conserved multiprotein complex required for the targeting and docking of post-Golgi vesicles to the plasma membrane. Through its interactions with a variety of proteins, including small GTPases, the exocyst is thought to integrate signals from the cell and signal that vesicles arriving at the plasma membrane are ready for fusion. Here we describe the three-dimensional crystal structure of one of the components of the exocyst, Exo70p, from Saccharomyces cerevisae at 3.5 angstrom resolution. Exo70p binds the small GTPase Rho3p in a GTP-dependent manner with an equilibrium dissociation constant of approximately 70 mu M. Exo70p is an extended rod approximately 155 A in length composed principally of alpha helices, and is a novel fold. The structure provides a first view of the Exo70 protein family and provides a framework to study the molecular function of this exocyst component. (c) 2005 Elsevier Ltd. All rights reserved.