5o8b

Difference-refined excited-state structure of rsEGFP2 1ps following 400nm-laser irradiation of the off-state.Difference-refined excited-state structure of rsEGFP2 1ps following 400nm-laser irradiation of the off-state.

Structural highlights 5o8b is a 1 chain structure with sequence from Aequorea victoria. 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: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMed Chromophores absorb light in photosensitive proteins and thereby initiate fundamental biological processes such as photosynthesis, vision and biofluorescence. An important goal in their understanding is the provision of detailed structural descriptions of the ultrafast photochemical events that they undergo, in particular of the excited states that connect chemistry to biological function. Here we report on the structures of two excited states in the reversibly photoswitchable fluorescent protein rsEGFP2. We populated the states through femtosecond illumination of rsEGFP2 in its non-fluorescent off state and observed their build-up (within less than one picosecond) and decay (on the several picosecond timescale). Using an X-ray free-electron laser, we performed picosecond time-resolved crystallography and show that the hydroxybenzylidene imidazolinone chromophore in one of the excited states assumes a near-canonical twisted configuration halfway between the trans and cis isomers. This is in line with excited-state quantum mechanics/molecular mechanics and classical molecular dynamics simulations. Our new understanding of the structure around the twisted chromophore enabled the design of a mutant that displays a twofold increase in its off-to-on photoswitching quantum yield. Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography.,Coquelle N, Sliwa M, Woodhouse J, Schiro G, Adam V, Aquila A, Barends TRM, Boutet S, Byrdin M, Carbajo S, De la Mora E, Doak RB, Feliks M, Fieschi F, Foucar L, Guillon V, Hilpert M, Hunter MS, Jakobs S, Koglin JE, Kovacsova G, Lane TJ, Levy B, Liang M, Nass K, Ridard J, Robinson JS, Roome CM, Ruckebusch C, Seaberg M, Thepaut M, Cammarata M, Demachy I, Field M, Shoeman RL, Bourgeois D, Colletier JP, Schlichting I, Weik M Nat Chem. 2018 Jan;10(1):31-37. doi: 10.1038/nchem.2853. Epub 2017 Sep 11. PMID:29256511 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

spinqualitylabelsall models 5o8b, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image