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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP
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Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP

机译：光诱导的蛋白裂解和荧光蛋白EosFP的绿色到红色转化的结构基础

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摘要

Genetically encoded fusion constructs derived from fluorescent proteins (FPs) can be designed to report on a multitude of events and signals in cells, tissues, and entire organs without interfering with the complex machinery of life. EosFP is a novel FIR from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with approximate to 400-nm light. This property enables localized tagging of proteins and thus provides a valuable tool for tracking protein movements within live cells. Here, we present the x-ray structures of the green and red forms of WT EosFP. They reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification.
机译：可以设计衍生自荧光蛋白（FPs）的遗传编码融合构建体，以报告细胞，组织和整个器官中的大量事件和信号，而不会干扰复杂的生命机制。 EosFP是一种新的FIR，来自巩膜珊瑚珊瑚Lobophyllia hemprichii，在用约400 nm的光照射后，其荧光发射从绿色（516 nm）切换为红色（581 nm）。该特性可以对蛋白质进行局部标记，从而为跟踪活细胞内蛋白质的运动提供了有价值的工具。在这里，我们介绍了WT EosFP的绿色和红色形式的X射线结构。他们揭示了红色发色团的形成与肽主链的切割有关，在结构的其他地方几乎没有什么变化，并为产生这种有趣的翻译后多肽修饰的机理提供了见识。

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