3P8U
Crystal structure of mEosFP in its green state
Summary for 3P8U
| Entry DOI | 10.2210/pdb3p8u/pdb |
| Related | 1ZUX 2BTJ 2VVH 2VVI 2VVJ |
| Descriptor | Green to red photoconvertible GPF-like protein EosFP, SULFITE ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | beta-barrel, fluorescent protein |
| Biological source | Lobophyllia hemprichii |
| Total number of polymer chains | 4 |
| Total formula weight | 108461.80 |
| Authors | Adam, V.,Nienhaus, G.U.,Bourgeois, D. (deposition date: 2010-10-15, release date: 2011-10-19, Last modification date: 2024-11-06) |
| Primary citation | Adam, V.,Moeyaert, B.,David, C.C.,Mizuno, H.,Lelimousin, M.,Dedecker, P.,Ando, R.,Miyawaki, A.,Michiels, J.,Engelborghs, Y.,Hofkens, J. Rational design of photoconvertible and biphotochromic fluorescent proteins for advanced microscopy applications. Chem.Biol., 18:1241-1251, 2011 Cited by PubMed Abstract: Advanced fluorescence imaging, including subdiffraction microscopy, relies on fluorophores with controllable emission properties. Chief among these fluorophores are the photoactivatable fluorescent proteins capable of reversible on/off photoswitching or irreversible green-to-red photoconversion. IrisFP was recently reported as the first fluorescent protein combining these two types of phototransformations. The introduction of this protein resulted in new applications such as super-resolution pulse-chase imaging. However, the spectroscopic properties of IrisFP are far from being optimal and its tetrameric organization complicates its use as a fusion tag. Here, we demonstrate how four-state optical highlighting can be rationally introduced into photoconvertible fluorescent proteins and develop and characterize a new set of such enhanced optical highlighters derived from mEosFP and Dendra2. We present in particular NijiFP, a promising new fluorescent protein with photoconvertible and biphotochromic properties that make it ideal for advanced fluorescence-based imaging applications. PubMed: 22035793DOI: 10.1016/j.chembiol.2011.08.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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