Crystal structure of the c-terminal domain of S. cerevisiae eIF5

Wei ZY; Xue YY; Xu H; Gong WM

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Crystal structure of the c-terminal domain of S. cerevisiae eIF5

机译：酿酒酵母eIF5 c端结构域的晶体结构

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eIF5, a GTPase-activating protein (GAP) specific for eIF2, plays a critical role in pre-initiation complex assembly and correct AUG selection during eukaryotic translation initiation. eIF5 is involved in the formation of the multifactor complex (MFC), an important intermediate of the 43 S pre-initiation complex. The C-terminal domain (CTD) of eIF5 functions as the structural core in the MFC assembly. Here we report the 1.5 A crystal structure of eIF5-CTD, confirming that eIF5-CTD contains an atypical HEAT motif. In addition, analyzing the electrostatic potential and the distribution of conserved residues on the protein surface, we confirm and suggest some potential regions of interactions between eIF5-CTD and other eIFs. The structure of eIF5-CTD provides useful information in understanding the mechanism of the MFC assembly. (c) 2006 Elsevier Ltd. All rights reserved.

机译：eIF5是一种对eIF2特异的GTP酶激活蛋白（GAP），在真核翻译起始过程中，在预起始复合物组装和正确选择AUG中起着关键作用。 eIF5参与了多因子复合物（MFC）的形成，这是43 S预起始复合物的重要中间体。 eIF5的C末端域（CTD）充当MFC组件中的结构核心。在这里，我们报告了eIF5-CTD的1.5 A晶体结构，证实了eIF5-CTD包含非典型的HEAT图案。此外，通过分析静电势和蛋白质表面上保守残基的分布，我们确认并提出了eIF5-CTD与其他eIF之间相互作用的一些潜在区域。 eIF5-CTD的结构为理解MFC组件的机制提供了有用的信息。（c）2006 Elsevier Ltd.保留所有权利。

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《Journal of Molecular Biology》 |2006年第1期|共9页
作者
Wei ZY; Xue YY; Xu H; Gong WM;
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正文语种 eng
中图分类分子生物学;
关键词
crystal structure; eIF5-CTD; multifactor complex; translation initiation; pre-initiation complex; TRANSLATION INITIATION; EUKARYOTIC TRANSLATION; IN-VIVO; PREINITIATION COMPLEX; MULTIFACTOR COMPLEX; BETA-SUBUNIT; HEAT DOMAIN; START CODON; PROTEIN; REFINEMENT;

机译：晶体结构;eIF5-CTD;多因子复合物;翻译起始;预起始复合物;翻译起始;真核翻译;体内;纯化复合物;多因子复合物;贝他取代基;热域;起始密码子;蛋白质;精制;

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1. Crystal structure of the c-terminal domain of S. cerevisiae eIF5 [J] . Wei ZY, Xue YY, Xu H, Journal of Molecular Biology . 2006,第1期

机译：酿酒酵母eIF5 c端结构域的晶体结构
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Crystal structure of the c-terminal domain of S. cerevisiae eIF5

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