2VVH

IrisFP fluorescent protein in its green form, cis conformation

Summary for 2VVH

• Entry DOI: 10.2210/pdb2vvh/pdb
• Related: 1ZUX 2BTJ 2VVI 2VVJ
• Descriptor: Green to red photoconvertible GFP-like protein EosFP, SULFATE ION, SULFITE ION, ... (4 entities in total)
• Functional Keywords: photoactivation, photoconversion, fluorescent protein, optical highlighters, microspectrophotometry, eosfp, photochromism, photoswitching
• Biological source: Lobophyllia hemprichii (Lobed brain coral)
• Total number of polymer chains: 4
• Total formula weight: 105722.98

Authors

Adam, V.,Lelimousin, M.,Boehme, S.,Desfonds, G.,Nienhaus, K.,Field, M.J.,Wiedenmann, J.,McSweeney, S.,Nienhaus, G.U.,Bourgeois, D. (deposition date: 2008-06-09, release date: 2008-11-11, Last modification date: 2024-11-06)

Primary citation

Adam, V.,Lelimousin, M.,Boehme, S.,Desfonds, G.,Nienhaus, K.,Field, M.J.,Wiedenmann, J.,Mcsweeney, S.,Nienhaus, G.U.,Bourgeois, D.
Structural Characterization of Irisfp, an Optical Highlighter Undergoing Multiple Photo-Induced Transformations.
Proc.Natl.Acad.Sci.USA, 105:18343-, 2008

PubMed Abstract: Photoactivatable fluorescent proteins (FPs) are powerful fluorescent highlighters in live cell imaging and offer perspectives for optical nanoscopy and the development of biophotonic devices. Two types of photoactivation are currently being distinguished, reversible photoswitching between fluorescent and nonfluorescent forms and irreversible photoconversion. Here, we have combined crystallography and (in crystallo) spectroscopy to characterize the Phe-173-Ser mutant of the tetrameric variant of EosFP, named IrisFP, which incorporates both types of phototransformations. In its green fluorescent state, IrisFP displays reversible photoswitching, which involves cis-trans isomerization of the chromophore. Like its parent protein EosFP, IrisFP also photoconverts irreversibly to a red-emitting state under violet light because of an extension of the conjugated pi-electron system of the chromophore, accompanied by a cleavage of the polypeptide backbone. The red form of IrisFP exhibits a second reversible photoswitching process, which may also involve cis-trans isomerization of the chromophore. Therefore, IrisFP displays altogether 3 distinct photoactivation processes. The possibility to engineer and precisely control multiple phototransformations in photoactivatable FPs offers exciting perspectives for the extension of the fluorescent protein toolkit.

PubMed: 19017808
DOI: 10.1073/PNAS.0805949105

Experimental method

X-RAY DIFFRACTION (1.8 Å)