4xtq | pdb_00004xtq

Crystal structure of a mutant (C20S) of a near-infrared fluorescent protein BphP1-FP

spinqualitylabelsall models 4xtq, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xtq is a 1 chain structure with sequence from Rhodopseudomonas palustris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: BL8, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Near-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes (BphPs) are the probes of choice for deep-tissue imaging. Detection of several processes requires spectrally distinct NIR FPs. We developed an NIR FP, BphP1-FP, which has the most blue-shifted spectra and the highest fluorescence quantum yield among BphP-derived FPs. We found that these properties result from the binding of the biliverdin chromophore to a cysteine residue in the GAF domain, unlike natural BphPs and other BphP-based FPs. To elucidate the molecular basis of the spectral shift, we applied biochemical, structural and mass spectrometry analyses and revealed the formation of unique chromophore species. Mutagenesis of NIR FPs of different origins indicated that the mechanism of the spectral shift is general and can be used to design multicolor NIR FPs from other BphPs. We applied pairs of spectrally distinct point cysteine mutants to multicolor cell labeling and demonstrated that they perform well in model deep-tissue imaging. Molecular Basis of Spectral Diversity in Near-Infrared Phytochrome-Based Fluorescent Proteins.,Shcherbakova DM, Baloban M, Pletnev S, Malashkevich VN, Xiao H, Dauter Z, Verkhusha VV Chem Biol. 2015 Nov 19;22(11):1540-51. doi: 10.1016/j.chembiol.2015.10.007. PMID:26590639 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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