7oo9
From Proteopedia
Structure of Chloroflexus islandicus LOV domain C85A variant (CisFbFP)
Structural highlights
FunctionPublication Abstract from PubMedLOV 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. References
|