Dronpa
From Proteopedia
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| - | <StructureSection load='2iov' size='350' side='right' scene='33/330991/Cv/ | + | <StructureSection load='2iov' size='350' side='right' scene='33/330991/Cv/8' caption='Fluorescent protein Dronpa complex with CYG chromophore [[2iov]]'> |
=== Function=== | === Function=== | ||
| - | '''Dronpa''' is a [[:Category:Gfp-like protein|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.”<ref name="webcite"> [http://www.brain.riken.jp/bsi-news/bsinews29/no29/research3e.html] (retrieved on November 30, 2008), </ref> 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<ref name="webcite" />. 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 <scene name='33/330991/Cv/ | + | '''Dronpa''' is a [[:Category:Gfp-like protein|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.”<ref name="webcite"> [http://www.brain.riken.jp/bsi-news/bsinews29/no29/research3e.html] (retrieved on November 30, 2008), </ref> 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<ref name="webcite" />. 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 <scene name='33/330991/Cv/9'>Beta-barrel</scene> structure. This reversible ability to be able to switch back and forth between “dark” and “light” is what makes Dronpa unique. See [[Colored & Bioluminescent Protein]]. |
=== Structural highlights=== | === Structural highlights=== | ||
| - | The amino acids that are key for this change - forming spontaneously the <scene name='33/330991/Cv/ | + | The amino acids that are key for this change - forming spontaneously the <scene name='33/330991/Cv/10'>CYG bicyclic chromophore - are Cys 62, Tyr 63, and Gly 64</scene>. There are also changes in conformation of four additional amino acids that are near the chromophore, <scene name='33/330991/Cv/11'>Arg 66, Ser 142, Val 157, and His 193</scene>. |
| + | *<scene name='33/330991/Cv/12'>Click here to see all contacts of chromophore</scene>. <ref>PMID:17117927</ref> | ||
</StructureSection> | </StructureSection> | ||
==3D structures of Dronpa== | ==3D structures of Dronpa== | ||
Revision as of 10:11, 10 March 2019
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3D structures of Dronpa
Updated on 10-March-2019
2ie2, 2iov, 2gx0, 2gx2, 3zuf, 3zuj, 3zul, 2z1o – EcFPD – Echinophyllia
4izn - EcFDP (mutant)
4uts - EcFDP (mutant) + chromophore Cys-Tyr-Gly
5hzs - EcFDP + chromophore Ser-Tyr-Gly + Co
5hzt - EcFDP + chromophore Ser-Tyr-Gly + Cu
5hzu - EcFDP + chromophore Ser-Tyr-Gly + Ni
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 Resources
For additional information, see: Colored & Bioluminescent Proteins
References
- ↑ 1.0 1.1 [1] (retrieved on November 30, 2008),
- ↑ Stiel AC, Trowitzsch S, Weber G, Andresen M, Eggeling C, Hell SW, Jakobs S, Wahl MC. 1.8 A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants. Biochem J. 2007 Feb 15;402(1):35-42. PMID:17117927 doi:10.1042/BJ20061401
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