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Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP

Nienhaus, K., Nienhaus, G.U., Wiedenmann, J. and Nar, H. (2005) Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP Proceedings of the National Academy of Sciences, 102, (26), pp. 9156-9159. (doi:10.1073/pnas.0501874102).

Record type: Article


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 FP from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with 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.

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Published date: 28 June 2005
Keywords: photochemistry, photoconversion, x-ray structure, Anthozoa
Organisations: Ocean and Earth Science


Local EPrints ID: 51184
ISSN: 0027-8424
PURE UUID: fb95075b-9c22-433e-b18d-bf717f59f3d5
ORCID for J. Wiedenmann: ORCID iD

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Date deposited: 08 May 2008
Last modified: 13 Jul 2017 16:32

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Author: K. Nienhaus
Author: G.U. Nienhaus
Author: J. Wiedenmann ORCID iD
Author: H. Nar

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