Dronpa

Function Dronpa is a GFP-like photoswitchable protein. It was first designed by Ryoko Ando, Hideaki Mizuno, and Atsushi Miyawaki in 2004. The protein was named after the “Japanese term Dron, a ninja term referring to instant disappearance of the body, and pa, short for photo activation.” Using a laser diode at 405nm the protein can be activated into its “bright” state, and using an argon laser at 480nm, the protein can be deactivated and turned into its “dark” state. Dronpa can be turned back and forth as often as necessary just by switching the wavelength of light that is focused onto it. Dronpa works by switching between the cis (bright state) to trans (dark state) position of a few amino acids in the chromophore center of the structure. This reversible ability to be able to switch back and forth between “dark” and “light” is what makes Dronpa unique. Structural highlights The amino acids that are key for this change - forming spontaneously the . There are also changes in conformation of four additional amino acids that are near the chromophore, . . .

spinqualitylabelsall models Fluorescent protein Dronpa complex with CYG chromophore 2iov Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of Dronpa3D structures of Dronpa

Updated on 05-January-2016

2ie2, 2iov, 2gx0, 2gx2, 3zuf, 3zuj, 3zul – EcFPD – Echinophyllia
4izn - EcFDP (mutant)
2z1o, 2z6y, 2z6z – EcFDP bright state
2pox – EcFDP dark state
4hq8, 4emq - EcFDP green-on state (mutant)
4hq9 - EcFDP green-off state (mutant)
4hqc - EcFDP red state (mutant)
2z6x – FDP - Pectiniidae

Additional ResourcesAdditional Resources

For additional information, see: Colored & Bioluminescent Proteins