Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan

被引：27

作者：

Buddha, MR ^{[1
]}

Crane, BR ^{[1
]}

机构：

[1] Cornell Univ, Dept Chem & Chem Biol, Ithaca, NY 14850 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 03期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

D O I：

10.1038/nsmb907

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 most divergent of two tryptophanyl tRNA synthetases (TrpRS II) found in Deinococcus radiodurans interacts with a nitric oxide synthase protein that produces 4-nitro-tryptophan (4-NRP). TrpRS II efficiently charges transfer RNA(Trp) with 4- NRP and 5-hydroxy-tryptophan (5-HRP). The crystal structures of TrpRS II bound to tryptophan and 5-HRP reveal residue substitutions that accommodate modified indoles. A class of auxiliary bacterial TrpRSs conserve this capacity to charge tRNA with nonstandard amino acids.

引用

页码：274 / 275

页数：2

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