4j88

Dark-state structure of sfGFP containing the unnatural amino acid p-azido-phenylalanine at residue 66

spinqualitylabelsall models 4j88, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j88 is a 2 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 2.08Å Ligands: CQ1, EDO, SO4, TRS 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 Expanding the genetic code opens new avenues to modulate protein function in real time. By genetically incorporating photoreactive phenyl azide, the fluorescent properties of green fluorescent protein (GFP) can be modulated by light. Depending on the residue in GFP programmed to incorporate the phenyl azide, different effects on function and photochemical pathways are observed. Different Photochemical Events of a Genetically Encoded Phenyl Azide Define and Modulate GFP Fluorescence.,Reddington SC, Rizkallah PJ, Watson PD, Pearson R, Tippmann EM, Jones DD Angew Chem Int Ed Engl. 2013 Apr 25. doi: 10.1002/anie.201301490. PMID:23620472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

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