The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold

被引：51

作者：

Nissen, P ^{[1
]}

Kjeldgaard, M ^{[1
]}

Thirup, S ^{[1
]}

Clark, BFC ^{[1
]}

Nyborg, J ^{[1
]}

机构：

[1] AARHUS UNIV, DEPT MOL & STRUCT BIOL, DK-8000 AARHUS C, DENMARK

来源：

BIOCHIMIE | 1996年 / 78卷 / 11-12期

关键词：

EF-Tu; aminoacyl-tRNA; ternary complex; recognition GTP;

D O I：

10.1016/S0300-9084(97)86714-4

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：

The refined crystal structure of the ternary complex of yeast Phe-tRNA(Phe), Thermus aquaticus elongation factor EF-Tu and the non-hydrolyzable GTP analog, GDPNP, reveals many details of the EF-Tu recognition of aminoacylated tRNA (aa-tRNA). EF-Tu-GTP recognizes the aminoacyl bond and one side of the backbone fold of the acceptor helix and has a high affinity for all ordinary elongator aa-tRNAs by binding to this aa-tRNA motif. Yet, the binding of deacylated tRNA, initiator tRNA, and selenocysteine-specific tRNA (tRNA(Sec)) is effectively discriminated against. Subtle rearrangements of the binding pocket may occur to optimize the fit to any side chain of the aminoacyl group and interactions with EF-Tu stabilize the 3'-aminoacyl isomer of aa-tRNA. A general complementarity is observed in the location of the binding sites in tRNA for synthetases and for EF-Tu. The complex formation is highly specific for the GTP-bound conformation of EF-Tu, which can explain the effects of various mutants.

引用

页码：921 / 933

页数：13

共 62 条

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