2otb
From Proteopedia
Crystal structure of a monomeric cyan fluorescent protein in the fluorescent state
Overview
Fluorescent protein (FP) variants that can be reversibly converted between fluorescent and nonfluorescent states have proven to be a catalyst for innovation in the field of fluorescence microscopy. However, the structural basis of the process remains poorly understood. High-resolution structures of a FP derived from Clavularia in both the fluorescent and the light-induced nonfluorescent states reveal that the rapid and complete loss of fluorescence observed upon illumination with 450-nm light results from cis-trans isomerization of the chromophore. The photoinduced change in configuration from the well ordered cis isomer to the highly nonplanar and disordered trans isomer is accompanied by a dramatic rearrangement of internal side chains. Taken together, the structures provide an explanation for the loss of fluorescence upon illumination, the slow light-independent recovery, and the rapid light-induced recovery of fluorescence. The fundamental mechanism appears to be common to all of the photoactivatable and reversibly photoswitchable FPs reported to date.
About this Structure
2OTB is a Single protein structure of sequence from Clavularia sp.. Full crystallographic information is available from OCA.
Reference
Structural basis for reversible photobleaching of a green fluorescent protein homologue., Henderson JN, Ai HW, Campbell RE, Remington SJ, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6672-7. Epub 2007 Apr 9. PMID:17420458 Page seeded by OCA on Sun May 4 11:36:54 2008
