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
收藏
页码：4805 / 4809
页数：5
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