3gj1

Publication Abstract from PubMed

Crystal structures of the photoactivatable green fluorescent protein T203H variant (PA-GFP) have been solved in the native and photoactivated states, which under 488 nm illumination are dark and brightly fluorescent, respectively. We demonstrate that photoactivation of PA-GFP is the result of a UV-induced decarboxylation of the Glu222 side chain that shifts the chromophore equilibrium to the anionic form. Coupled with the T203H mutation, which stabilizes the native PA-GFP neutral chromophore, Glu222 decarboxylation yields a 100-fold contrast enhancement relative to wild-type GFP (WT). Additionally, the structures provide insights into the spectroscopic differences between WT and PA-GFP steady-state fluorescence maxima and excited-state proton transfer dynamics.

Structure and Mechanism of the Photoactivatable Green Fluorescent Protein.,Henderson JN, Gepshtein R, Heenan JR, Kallio K, Huppert D, Remington SJ J Am Chem Soc. 2009 Mar 11. PMID:19278226^[1]

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