Document Detail

Structural basis for reversible photobleaching of a green fluorescent protein homologue.
MedLine Citation:
PMID:  17420458     Owner:  NLM     Status:  MEDLINE    
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.
J Nathan Henderson; Hui-Wang Ai; Robert E Campbell; S James Remington
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-04-09
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  104     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-18     Completed Date:  2007-06-06     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6672-7     Citation Subset:  IM    
Departments of Chemistry and Physics, and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
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MeSH Terms
Crystallography, X-Ray
Directed Molecular Evolution
Green Fluorescent Proteins / chemistry*,  metabolism*
Protein Engineering*
Structural Homology, Protein*
Grant Support
Reg. No./Substance:
0/Cyan Fluorescent Protein; 147336-22-9/Green Fluorescent Proteins

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