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6ukl

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Crystal Structure of a DiB2-split Protein

Structural highlights

6ukl is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.02Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLC_ECOLI Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids.^[1]

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^[2]

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

References

↑ Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C. The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding. FEBS Lett. 2004 Mar 26;562(1-3):183-8. PMID:15044022 doi:10.1016/S0014-5793(04)00199-1
↑ 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