Structural basis of tRNA agmatinylation essential for AUA codon decoding

被引：0

作者：

Takuo Osawa

Satoshi Kimura

Naohiro Terasaka

Hideko Inanaga

Tsutomu Suzuki

Tomoyuki Numata

机构：

[1] Biomedical Research Institute,Department of Chemistry and Biotechnology

[2] National Institute of Advanced Industrial Science and Technology (AIST),undefined

[3] Graduate School of Engineering,undefined

[4] University of Tokyo,undefined

[5] Precursory Research for Embryonic Science and Technology (PRESTO),undefined

[6] Japan Science and Technology Agency (JST),undefined

来源：

Nature Structural & Molecular Biology | 2011年 / 18卷

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D O I：

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中图分类号：

学科分类号：

摘要：

TiaS catalyzes the transfer of agmatine onto the first position cytidine of the tRNAIle2 anticodon in archaea, ensuring proper translation of the matching codon. Now the crystal structures of the TiaS–tRNAIle2 complex with ATP, or with AMPCPP and agmatine, reveal a novel kinase domain and show how TiaS selects the correct tRNA while segregating the target cytidine until agmatine is bound.

引用

页码：1275 / 1280

页数：5

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