2ie2

The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein

spinqualitylabelsall models 2ie2, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ie2 is a 6 chain structure with sequence from Echinophyllia sp. SC22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: GYC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5TLG6_9CNID Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The green fluorescent protein (GFP), its variants, and the closely related GFP-like proteins possess a wide variety of spectral properties that are of widespread interest as biological tools. One desirable spectral property, termed photoswitching, involves the light-induced alteration of the optical properties of certain GFP members. Although the structural basis of both reversible and irreversible photoswitching events have begun to be unraveled, the mechanisms resulting in reversible photoswitching are less clear. A novel GFP-like protein, Dronpa, was identified to have remarkable light-induced photoswitching properties, maintaining an almost perfect reversible photochromic behavior with a high fluorescence to dark state ratio. We have crystallized and subsequently determined to 1.7 A resolution the crystal structure of the fluorescent state of Dronpa. The chromophore was observed to be in its anionic form, adopting a cis co-planar conformation. Comparative structural analysis of non-photoactivatable and photoactivatable GFPs, together with site-directed mutagenesis of a position (Cys62) within the Dronpa chromophore, has provided a basis for understanding Dronpa photoactivation. Specifically, we propose a model of reversible photoactivation whereby irradiation with light leads to subtle conformational changes within and around the environment of the chromophore that promotes proton transfer along an intricate polar network. The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein.,Wilmann PG, Turcic K, Battad JM, Wilce MC, Devenish RJ, Prescott M, Rossjohn J J Mol Biol. 2006 Nov 24;364(2):213-24. Epub 2006 Sep 3. PMID:17010376 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dronpa Green Fluorescent Protein 3D structures

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