6AA7
Fluorescent protein from Acropora digitifera
Summary for 6AA7
| Entry DOI | 10.2210/pdb6aa7/pdb |
| Descriptor | Fluorescent protein (2 entities in total) |
| Functional Keywords | fluorescent protein, red fluorescent protein, acropora digitifera, chromophore |
| Biological source | Acropora digitifera (Staghorn coral) |
| Total number of polymer chains | 2 |
| Total formula weight | 52840.48 |
| Authors | Kim, S.E.,Hwang, K.Y.,Nam, K.H. (deposition date: 2018-07-17, release date: 2018-08-22, Last modification date: 2024-10-09) |
| Primary citation | Kim, S.E.,Hwang, K.Y.,Nam, K.H. Spectral and structural analysis of a red fluorescent protein from Acropora digitifera. Protein Sci., 28:375-381, 2019 Cited by PubMed Abstract: 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. PubMed: 30368951DOI: 10.1002/pro.3540 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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