Structure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNA

被引：54

作者：

Schmitt, Emmanuelle ^{[1
]}

Panverti, Michel ^{[1
]}

Lazennec-Schurdevin, Christine ^{[1
]}

Coureux, Pierre-Damien ^{[1
]}

Perez, Javier ^{[2
]}

Thompson, Andrew ^{[2
]}

Mechulam, Yves ^{[1
]}

机构：

[1] Ecole Polytech, CNRS, Unite Mixte Rech 7654, Biochim Lab, F-91128 Palaiseau, France

[2] SOLEIL Synchrotron, Gif Sur Yvette, France

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 04期

关键词：

EUKARYOTIC TRANSLATION INITIATION; START-SITE SELECTION; CRYSTAL-STRUCTURE; FACTOR EIF2-GAMMA; GTP HYDROLYSIS; ALPHA-SUBUNIT; GAMMA-SUBUNIT; BETA-SUBUNIT; FACTOR EIF2; BINDING;

D O I：

10.1038/nsmb.2259

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Eukaryotic and archaeal translation initiation factor 2 (e/aIF2) is a heterotrimeric GTPase that has a crucial role in the selection of the correct start codon on messenger RNA. We report the 5-angstrom resolution crystal structure of the ternary complex formed by archaeal aIF2 from Sulfolobus solfataricus, the GTP analog GDPNP and methionylated initiator tRNA. The 3D model is further supported by solution studies using small-angle X-ray scattering. The tRNA is bound by the alpha and gamma subunits of aIF2. Contacts involve the elbow of the tRNA and the minor groove of the acceptor stem, but not the T-stem minor groove. We conclude that despite considerable structural homology between the core gamma subunit of aIF2 and the elongation factor EF1A, these two G proteins of the translation apparatus use very different tRNA-binding strategies.

引用

页码：450 / 454

页数：5

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