3WCK
Crystal structure of monomeric photosensitizing fluorescent protein, Supernova
Summary for 3WCK
| Entry DOI | 10.2210/pdb3wck/pdb |
| Descriptor | Monomeric photosenitizing fluorescent protein supernova (2 entities in total) |
| Functional Keywords | gfp fold, fluorescent protein, genetically encoded photosensitizer, phototoxicity |
| Biological source | synthetic construct |
| Total number of polymer chains | 8 |
| Total formula weight | 242806.86 |
| Authors | Sakai, N.,Matsuda, T.,Takemoto, K.,Nagai, T. (deposition date: 2013-05-27, release date: 2013-10-02, Last modification date: 2024-11-20) |
| Primary citation | Takemoto, K.,Matsuda, T.,Sakai, N.,Fu, D.,Noda, M.,Uchiyama, S.,Kotera, I.,Arai, Y.,Horiuchi, M.,Fukui, K.,Ayabe, T.,Inagaki, F.,Suzuki, H.,Nagai, T. SuperNova, a monomeric photosensitizing fluorescent protein for chromophore-assisted light inactivation Sci Rep, 3:2629-2629, 2013 Cited by PubMed Abstract: Chromophore-assisted light inactivation (CALI) is a powerful technique for acute perturbation of biomolecules in a spatio-temporally defined manner in living specimen with reactive oxygen species (ROS). Whereas a chemical photosensitizer including fluorescein must be added to specimens exogenously and cannot be restricted to particular cells or sub-cellular compartments, a genetically-encoded photosensitizer, KillerRed, can be controlled in its expression by tissue specific promoters or subcellular localization tags. Despite of this superiority, KillerRed hasn't yet become a versatile tool because its dimerization tendency prevents fusion with proteins of interest. Here, we report the development of monomeric variant of KillerRed (SuperNova) by direct evolution using random mutagenesis. In contrast to KillerRed, SuperNova in fusion with target proteins shows proper localization. Furthermore, unlike KillerRed, SuperNova expression alone doesn't perturb mitotic cell division. Supernova retains the ability to generate ROS, and hence promote CALI-based functional analysis of target proteins overcoming the major drawbacks of KillerRed. PubMed: 24043132DOI: 10.1038/srep02629 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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