2GX0

Crystal structural and functional analysis of GFP-like fluorescent protein

Summary for 2GX0

• Entry DOI: 10.2210/pdb2gx0/pdb
• Related: 2GX2
• Descriptor: fluorescent protein Dronpa (2 entities in total)
• Functional Keywords: fluorescence, b-can, photoswitching, luminescent protein
• Biological source: Echinophyllia sp. SC22 (coral)
• Total number of polymer chains: 4
• Total formula weight: 110453.18

Authors

Hwang, K.Y.,Nam, K.-H.,Park, S.-Y.,Sugiyama, K. (deposition date: 2006-05-08, release date: 2007-05-08, Last modification date: 2024-10-09)

Primary citation

Nam, K.-H.,Kwon, O.Y.,Sugiyama, K.,Lee, W.-H.,Kim, Y.K.,Song, H.K.,Kim, E.E.,Park, S.-Y.,Jeon, H.,Hwang, K.Y.
Structural characterization of the photoswitchable fluorescent protein Dronpa-C62S
Biochem.Biophys.Res.Commun., 354:962-967, 2007

PubMed Abstract: 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.

PubMed: 17276392
DOI: 10.1016/j.bbrc.2007.01.086

Experimental method

X-RAY DIFFRACTION (1.9 Å)