6aa7

Fluorescent protein from Acropora digitifera

spinqualitylabelsall models 6aa7, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6aa7 is a 2 chain structure with sequence from Acropora digitifera. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: XYG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1S7IWI8_ACRDI Publication Abstract from PubMed Fluorescent proteins (FPs) possess a wide variety of spectral properties that make them of widespread interest as optical markers. These proteins can be applied as pH indicators or metal biosensors. The discovery and characterization of new fluorescent proteins is expected to further extend their application. Here, we report the spectral and structural analysis of a red fluorescent protein from Acropora digitifera (designated AdRed). This protein shows a tetrameric state and is red emitting, with excitation and emission maxima at 567 and 612 nm, respectively. Its crystal structure shows the tetrameric interface stabilized by hydrogen bonding and salt bridges. The electron density map of the chromophore, consisting of Asp66-Tyr67-Gly68, shows the decarboxylated side chain of Asp66. Ser223, located near the chromophore, has the role of bridging His202 and Glu221, and is part of the hydrogen bond network. Mutated AdRed with Cys148Ser reveals a blue shift in fluorescence excitation and emission. Our results provide insights into understanding the molecular function of AdRed and other FPs. Spectral and structural analysis of a red fluorescent protein from Acropora digitifera.,Kim SE, Hwang KY, Nam KH Protein Sci. 2019 Feb;28(2):375-381. doi: 10.1002/pro.3540. Epub 2018 Nov 27. PMID:30368951 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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