Structural highlights
Function
[BLC_ECO57] Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids (By similarity).
Publication Abstract from PubMed
Fluorogen-activating proteins (FAPs) are innovative fluorescent probes combining advantages of genetically-encoded proteins such as green fluorescent protein and externally added fluorogens that allow for highly tunable and on demand fluorescent signaling. Previously, a panel of green- and red-emitting FAPs has been created from bacterial lipocalin Blc (named DiBs). Here we present a rational design as well as functional and structural characterization of the first self-assembling FAP split system, DiB-splits. This new system decreases the size of the FAP label to ~8-12 kDa while preserving DiBs' unique properties: strong increase in fluorescence intensity of the chromophore upon binding, binding affinities to the chromophore in nanomolar to low micromolar range, and high photostability of the protein-ligand complex. These properties allow for use of DiB-splits for wide-field, confocal, and super-resolution fluorescence microscopy. DiB-splits also represent an attractive starting point for further design of a protein-protein interaction detection system as well as novel FAP-based sensors.
DiB-splits: nature-guided design of a novel fluorescent labeling split system.,Bozhanova NG, Gavrikov AS, Mishin AS, Meiler J Sci Rep. 2020 Jul 6;10(1):11049. doi: 10.1038/s41598-020-67095-2. PMID:32632329[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bozhanova NG, Gavrikov AS, Mishin AS, Meiler J. DiB-splits: nature-guided design of a novel fluorescent labeling split system. Sci Rep. 2020 Jul 6;10(1):11049. doi: 10.1038/s41598-020-67095-2. PMID:32632329 doi:http://dx.doi.org/10.1038/s41598-020-67095-2
