7OO9
Structure of Chloroflexus islandicus LOV domain C85A variant (CisFbFP)
Summary for 7OO9
| Entry DOI | 10.2210/pdb7oo9/pdb |
| Descriptor | Hybrid sensor histidine kinase/response regulator, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | flavin, fluorescent protein |
| Biological source | Chloroflexus islandicus |
| Total number of polymer chains | 2 |
| Total formula weight | 26947.88 |
| Authors | Gushchin, I.,Remeeva, A.,Goncharov, I.M. (deposition date: 2021-05-26, release date: 2021-06-30, Last modification date: 2024-01-31) |
| Primary citation | Goncharov, I.M.,Smolentseva, A.,Semenov, O.,Natarov, I.,Nazarenko, V.V.,Yudenko, A.,Remeeva, A.,Gushchin, I. High-resolution structure of a naturally red-shifted LOV domain. Biochem.Biophys.Res.Commun., 567:143-147, 2021 Cited by PubMed Abstract: LOV domains are widespread photosensory modules that have also found applications in fluorescence microscopy, optogenetics, and light-driven generation of reactive oxygen species. Many of these applications require stable proteins with altered spectra. Here, we report a flavin-based fluorescent protein CisFbFP derived from Chloroflexus islandicus LOV domain-containing protein. We show that CisFbFP is thermostable, and its absorption and fluorescence spectra are red-shifted for ∼6 nm, which has not been observed for other cysteine-substituted natural LOV domains. We also provide a crystallographic structure of CisFbFP at the resolution of 1.2 Å that reveals alterations in the active site due to replacement of conservative asparagine with a serine. Finally, we discuss the possible effects of presence of cis-proline in the Aβ-Bβ loop on the protein's structure and stability. The findings provide the basis for engineering and color tuning of LOV-based tools for molecular biology. PubMed: 34153684DOI: 10.1016/j.bbrc.2021.06.046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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