The rotational order-disorder structure of the reversibly photoswitchable red fluorescent protein rsTagRFP.
نویسندگان
چکیده
The rotational order-disorder (OD) structure of the reversibly photoswitchable fluorescent protein rsTagRFP is discussed in detail. The structure is composed of tetramers of 222 symmetry incorporated into the lattice in two different orientations rotated 90° with respect to each other around the crystal c axis and with tetramer axes coinciding with the crystallographic twofold axes. The random distribution of alternatively oriented tetramers in the crystal creates the rotational OD structure with statistically averaged I422 symmetry. Despite order-disorder pathology, the structure of rsTagRFP has electron-density maps of good quality for both non-overlapping and overlapping parts of the model. The crystal contacts, crystal internal architecture and a possible mechanism of rotational OD crystal formation are discussed.
منابع مشابه
Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET.
We have developed the first red fluorescent protein, named rsTagRFP, which possesses reversibly photoswitchable absorbance spectra. Illumination with blue and yellow light switches rsTagRFP into a red fluorescent state (ON state) or nonfluorescent state (OFF state), respectively. The ON and OFF states exhibit absorbance maxima at 567 and 440 nm, respectively. Due to the photoswitchable absorban...
متن کاملA structural basis for reversible photoswitching of absorbance spectra in red fluorescent protein rsTagRFP.
rsTagRFP is the first monomeric red fluorescent protein (FP) with reversibly photoswitchable absorbance spectra. The switching is realized by irradiation of rsTagRFP with blue (440 nm) and yellow (567 nm) light, turning the protein fluorescence ON and OFF, respectively. It is perhaps the most useful probe in this color class that has yet been reported. Because of the photoswitchable absorbance,...
متن کاملPhotoswitchable Spiropyran Dyads for Biological Imaging
The synthesis of a small-molecule dyad consisting of a far-red-emitting silicon rhodamine dye that is covalently linked to a photochromic spironaphthothiopyran unit, which serves as a photoswitchable quencher, is reported. This system can be switched reversibly between the fluorescent and nonfluorescent states using visible light at wavelengths of 405 and 630 nm, respectively, and it works effe...
متن کاملPhotosynthetic Electron Transport
Bizzarri R, Serresi M, Cardarelli F, Abbruzzetti S, Campanini B, Viappiani C, Beltram F. Single amino acid replacement makes Aequorea victoria fluorescent proteins reversibly photoswitchable. J Am Chem Soc. 2010;132:85–95. Cardarelli F, Bizzarri R, Serresi M, Albertazzi L, Beltram F. Probing nuclear localization signal-importin alpha binding equilibria in living cells. J Biol Chem. 2009;284:366...
متن کاملA photochromic and thermochromic fluorescent protein
Photochromism is a change of colour induced by irradiation with light, while thermochromism is a change of colour due to a change of temperature. Both photochromism and thermochromism have been observed in inorganic and organic compounds, however thermochromism is much less common in biological systems. One mechanism by which molecular photochromism can occur is a photo-induced isomerization to...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 70 Pt 1 شماره
صفحات -
تاریخ انتشار 2014