Significant Expansion of the Fluorescent Protein Chromophore through the Genetic Incorporation of a Metal-Chelating Unnatural Amino Acid

被引：72

作者：

Liu, Xiaohong ^{[1
]}

Li, Jiasong ^{[1
,2
]}

Hu, Cheng ^{[1
]}

Zhou, Qing ^{[1
]}

Zhang, Wei ^{[1
]}

Hu, Meirong ^{[1
]}

Zhou, Juanzuo ^{[1
]}

Wang, Jiangyun ^{[1
]}

机构：

[1] Chinese Acad Sci, Lab Noncoding RNA, Inst Biophys, Beijing 100101, Peoples R China

[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 18期

基金：

美国国家科学基金会;

关键词：

amino acids; fluorescent proteins; genetic-code expansion; metal-chelating amino acids; metalloenzymes; CROSS-LINK; DYNAMICS; SENSORS; SITE;

D O I：

10.1002/anie.201301307

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Caught red-shifted: A novel metal-chelating unnatural amino acid with an 8-hydroxyquinoline group (HqAla) can be enzymatically incorporated into GFP (see scheme). Substituting a Tyr residue in the chromophore of FPs with HqAla results in significantly red-shifted excitation and emission maxima. The crystal structure of superfolder GFP bearing HqAla in its chromophore shows the structural basis for these red shifts. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：4805 / 4809

页数：5