1zux

EosFP Fluorescent Protein- Green Form

spinqualitylabelsall models 1zux, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zux is a 4 chain structure with sequence from Lobophyllia hemprichii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CR8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5S6Z9_LOBHE Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP.,Nienhaus K, Nienhaus GU, Wiedenmann J, Nar H Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9156-9. Epub 2005 Jun 17. PMID:15964985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

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