View source for 6ukk


==Crystal Structure of a Domain-swapped Fluorogen Activating Protein DiB3 Dimer==
<StructureSection load='6ukk' size='340' side='right'caption='[[6ukk]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ukk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UKK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ukk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ukk OCA], [https://pdbe.org/6ukk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ukk RCSB], [https://www.ebi.ac.uk/pdbsum/6ukk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ukk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLC_ECOLI BLC_ECOLI] Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids.<ref>PMID:15044022</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:32632329</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ukk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bozhanova NG]]
[[Category: Meiler J]]