Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase
Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase
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DOI：
10.1021/ja0549042
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发表时间：
2005-11-02
影响因子：
15
通讯作者：
Schultz, PG
中科院分区：
文献类型：
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作者：
Turner, JM;Graziano, J;Schultz, PG
最近的研究表明，正交 tRNA/氨酰基-tRNA 合成酶对可以进化成允许将非天然氨基酸遗传掺入原核生物和真核生物的蛋白质中。在这里，我们描述了一种进化的氨酰基-tRNA合成酶的晶体结构，该合成酶负责加载非天然氨基酸对乙酰基苯丙氨酸。分子识别是由于侧链和主链构象的变化导致氢键和与结合底物的堆积相互作用的改变。
It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acidp-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.