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Publication Abstract from PubMed

The photoswitching behavior of green fluorescent proteins (GFPs) or GFP-like proteins is increasingly recognized as a new technique for optical marking. Recently, Ando and his colleagues developed a new green fluorescent protein Dronpa, which possesses the unique photochromic property of being photoswitchable in a non-destructive manner. To better understand this mechanism, we determined the crystal structures of a new GFP Dronpa and its mutant C62S, at 1.9 Angstroms and 1.8 Angstroms, respectively. Determination of the structures demonstrates that a unique hydrogen-bonding network and the sulfur atom of the chromophore are critical to the photoswitching property of Dronpa. Reversible photoswitching was lost in cells expressing the Dronpa-C62S upon repetitive irradiation compared to the native protein. Structural and mutational analyses reveal the chemical basis for the functional properties of photoswitchable fluorescent proteins and provide the basis for subsequent coherent engineering of this subfamily of Dronpa homologs.

Structural characterization of the photoswitchable fluorescent protein Dronpa-C62S.,Nam KH, Kwon OY, Sugiyama K, Lee WH, Kim YK, Song HK, Kim EE, Park SY, Jeon H, Hwang KY Biochem Biophys Res Commun. 2007 Mar 23;354(4):962-7. Epub 2007 Jan 24. PMID:17276392^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.