The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5
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DOI：
10.1016/j.jmb.2006.05.021
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发表时间：
2006-07-07
影响因子：
5.6
通讯作者：
Baumann, Ulrich
中科院分区：
文献类型：
--
作者：
Bieniossek, Christoph;Schuetz, Patrick;Baumann, Ulrich
真核起始因子5 （eIF5）的羧基末端结构域（CTD）在多因子复合物（MFC）的形成中起核心作用，MFC是43 S预起始复合物组装的重要中间体。IF5-CTD直接与翻译起始因子eIF1、eIF2-Met β和eIF3c相互作用，从而与eIF2结合的Met- trna (i)（Met）一起形成MFC。在这项工作中，我们提出了高分辨率的晶体结构的eIF5-CTD。该蛋白的结构域完全由α -螺旋组成，与weIF2B-epsilon （eIF2B epsilon-CTD）的羧基末端结构域同源。这两种结构最显著的区别是eIF5中有一个额外的羧基末端螺旋。eif2 - β、eIF3和eIF1的结合位点被映射到该结构上。eif2 - β和eIF3分别结合到负和正静电电位的非重叠斑块上。(c) 2006 Elsevier Ltd.版权所有。
The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S preinitiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-Met beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed Out of alpha-helices and is homologous to the carboxy-terminal domain of weIF2B-epsilon (eIF2B epsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively. (c) 2006 Elsevier Ltd. All rights reserved.