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1ZUX

EosFP Fluorescent Protein- Green Form

Summary for 1ZUX
Entry DOI10.2210/pdb1zux/pdb
Related2btj
Descriptorgreen to red photoconvertible GPF-like protein EosFP (2 entities in total)
Functional Keywordsfluorescent protein, photoconversion, peptide bond cleavage, beta-elimination, luminescent protein
Biological sourceLobophyllia hemprichii
Total number of polymer chains4
Total formula weight103229.03
Authors
Nar, H.,Nienhaus, K.,Wiedenmann, J.,Nienhaus, G.U. (deposition date: 2005-06-01, release date: 2005-06-28, Last modification date: 2024-11-06)
Primary citationNienhaus, K.,Nienhaus, G.U.,Wiedenmann, J.,Nar, H.
Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP.
Proc.Natl.Acad.Sci.Usa, 102:9156-9159, 2005
Cited by
PubMed Abstract: 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 approximately 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.
PubMed: 15964985
DOI: 10.1073/pnas.0501874102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

229380

數據於2024-12-25公開中

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