3ST3
Dreiklang - off state
Summary for 3ST3
Entry DOI | 10.2210/pdb3st3/pdb |
Related | 1HUY 3ST2 3ST4 |
Descriptor | Dreiklang, PHOSPHATE ION (3 entities in total) |
Functional Keywords | gfp-like, beta barrel, reversibly switchable fluorescent protein, anthozoa, fluorescent dyes, luminescent protein, fluorescent protein |
Biological source | Aequorea victoria |
Total number of polymer chains | 3 |
Total formula weight | 86909.41 |
Authors | Brakemann, T.,Weber, G.,Andresen, M.,Stiel, A.C.,Jakobs, S.,Wahl, M.C. (deposition date: 2011-07-08, release date: 2011-09-14, Last modification date: 2024-10-30) |
Primary citation | Brakemann, T.,Stiel, A.C.,Weber, G.,Andresen, M.,Testa, I.,Grotjohann, T.,Leutenegger, M.,Plessmann, U.,Urlaub, H.,Eggeling, C.,Wahl, M.C.,Hell, S.W.,Jakobs, S. A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching. Nat.Biotechnol., 29:942-947, 2011 Cited by PubMed Abstract: Photoswitchable fluorescent proteins have enabled new approaches for imaging cells, but their utility has been limited either because they cannot be switched repeatedly or because the wavelengths for switching and fluorescence imaging are strictly coupled. We report a bright, monomeric, reversibly photoswitchable variant of GFP, Dreiklang, whose fluorescence excitation spectrum is decoupled from that for optical switching. Reversible on-and-off switching in living cells is accomplished at illumination wavelengths of ∼365 nm and ∼405 nm, respectively, whereas fluorescence is elicited at ∼515 nm. Mass spectrometry and high-resolution crystallographic analysis of the same protein crystal in the photoswitched on- and off-states demonstrate that switching is based on a reversible hydration/dehydration reaction that modifies the chromophore. The switching properties of Dreiklang enable far-field fluorescence nanoscopy in living mammalian cells using both a coordinate-targeted and a stochastic single molecule switching approach. PubMed: 21909082DOI: 10.1038/nbt.1952 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.702 Å) |
Structure validation
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