 |
PDBsum entry 2gx0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Luminescent protein
|
PDB id
|
|
|
|
2gx0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural characterization of the photoswitchable fluorescent protein dronpa-C62s.
|
|
|
Authors
|
|
K.H.Nam,
O.Y.Kwon,
K.Sugiyama,
W.H.Lee,
Y.K.Kim,
H.K.Song,
E.E.Kim,
S.Y.Park,
H.Jeon,
K.Y.Hwang.
|
|
|
Ref.
|
|
Biochem Biophys Res Commun, 2007,
354,
962-967.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The photoswitching behavior of green fluorescent proteins (GFPs) or GFP-like
proteins is increasingly recognized as a new technique for optical marking.
Recently, Ando and his colleagues developed a new green fluorescent protein
Dronpa, which possesses the unique photochromic property of being
photoswitchable in a non-destructive manner. To better understand this
mechanism, we determined the crystal structures of a new GFP Dronpa and its
mutant C62S, at 1.9 Angstroms and 1.8 Angstroms, respectively. Determination of
the structures demonstrates that a unique hydrogen-bonding network and the
sulfur atom of the chromophore are critical to the photoswitching property of
Dronpa. Reversible photoswitching was lost in cells expressing the Dronpa-C62S
upon repetitive irradiation compared to the native protein. Structural and
mutational analyses reveal the chemical basis for the functional properties of
photoswitchable fluorescent proteins and provide the basis for subsequent
coherent engineering of this subfamily of Dronpa homologs.
|
|
|
|
|
|
|
