2OTB

Crystal structure of a monomeric cyan fluorescent protein in the fluorescent state

Summary for 2OTB

• Entry DOI: 10.2210/pdb2otb/pdb
• Related: 2OTE
• Descriptor: GFP-like fluorescent chromoprotein cFP484 (2 entities in total)
• Functional Keywords: beta can, fluorescent protein
• Biological source: Clavularia sp.
• Total number of polymer chains: 2
• Total formula weight: 49598.37

Authors

Henderson, J.N.,Ai, H.,Campbell, R.E.,Remington, S.J. (deposition date: 2007-02-07, release date: 2007-04-03, Last modification date: 2023-11-15)

Primary citation

Henderson, J.N.,Ai, H.W.,Campbell, R.E.,Remington, S.J.
Structural basis for reversible photobleaching of a green fluorescent protein homologue.
Proc.Natl.Acad.Sci.Usa, 104:6672-6677, 2007

PubMed Abstract: 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.

PubMed: 17420458
DOI: 10.1073/pnas.0700059104

Experimental method

X-RAY DIFFRACTION (1.79 Å)