Turner James M, Graziano James, Spraggon Glen, Schultz Peter G
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.
J Am Chem Soc. 2005 Nov 2;127(43):14976-7. doi: 10.1021/ja0549042.
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 acid p-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.
最近研究表明，正交tRNA/氨酰tRNA合成酶对能够经过进化，从而在原核生物和真核生物中实现将非天然氨基酸遗传掺入蛋白质中。在此，我们描述了一种进化后的氨酰tRNA合成酶的晶体结构，该酶负责将非天然氨基酸对乙酰基苯丙氨酸进行氨酰化。分子识别归因于侧链和主链构象变化导致的与结合底物的氢键和堆积相互作用的改变。
