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Publication Abstract from PubMed

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 approximately 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 A 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 Abeta-Bbeta 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.

High-resolution structure of a naturally red-shifted LOV domain.,Goncharov IM, Smolentseva A, Semenov O, Natarov I, Nazarenko VV, Yudenko A, Remeeva A, Gushchin I Biochem Biophys Res Commun. 2021 Jun 18;567:143-147. doi:, 10.1016/j.bbrc.2021.06.046. PMID:34153684^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.