7DIG
Green fluorescent protein from Dendronephthya sp. SSAL-2002
Summary for 7DIG
| Entry DOI | 10.2210/pdb7dig/pdb |
| Descriptor | Green fluorescent protein (1 entity in total) |
| Functional Keywords | dendra, dendronephthya, fluorescent protein, gfp |
| Biological source | Dendronephthya sp. SSAL-2002 |
| Total number of polymer chains | 8 |
| Total formula weight | 206578.54 |
| Authors | Nam, K.H. (deposition date: 2020-11-19, release date: 2021-12-08, Last modification date: 2024-10-23) |
| Primary citation | Kim, I.J.,Xu, Y.,Nam, K.H. Metal-Induced Fluorescence Quenching of Photoconvertible Fluorescent Protein DendFP. Molecules, 27:-, 2022 Cited by PubMed Abstract: Sensitive and accurate detection of specific metal ions is important for sensor development and can advance analytical science and support environmental and human medical examinations. Fluorescent proteins (FPs) can be quenched by specific metal ions and spectroscopically show a unique fluorescence-quenching sensitivity, suggesting their potential application as FP-based metal biosensors. Since the characteristics of the fluorescence quenching are difficult to predict, spectroscopic analysis of new FPs is important for the development of FP-based biosensors. Here we reported the spectroscopic and structural analysis of metal-induced fluorescence quenching of the photoconvertible fluorescent protein DendFP. The spectroscopic analysis showed that Fe, Fe, and Cu significantly reduced the fluorescence emission of DendFP. The metal titration experiments showed that the dissociation constants () of Fe, Fe, and Cu for DendFP were 24.59, 41.66, and 137.18 μM, respectively. The tetrameric interface of DendFP, which the metal ions cannot bind to, was analyzed. Structural comparison of the metal-binding sites of DendFP with those of iq-mEmerald and Dronpa suggested that quenchable DendFP has a unique metal-binding site on the β-barrel that does not utilize the histidine pair for metal binding. PubMed: 35566273DOI: 10.3390/molecules27092922 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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