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6ukk
From Proteopedia
(Difference between revisions)
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==Crystal Structure of a Domain-swapped Fluorogen Activating Protein DiB3 Dimer== | ==Crystal Structure of a Domain-swapped Fluorogen Activating Protein DiB3 Dimer== | ||
| - | <StructureSection load='6ukk' size='340' side='right'caption='[[6ukk]]' scene=''> | + | <StructureSection load='6ukk' size='340' side='right'caption='[[6ukk]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=6UKK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ukk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6UKK FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ukk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ukk OCA], [http://pdbe.org/6ukk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ukk RCSB], [http://www.ebi.ac.uk/pdbsum/6ukk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ukk ProSAT]</span></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blc, Z5756, ECs5130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ukk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ukk OCA], [http://pdbe.org/6ukk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ukk RCSB], [http://www.ebi.ac.uk/pdbsum/6ukk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ukk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BLC_ECO57 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). | ||
| + | <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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bozhanova | + | [[Category: Bozhanova, N G]] |
| - | [[Category: Meiler J]] | + | [[Category: Meiler, J]] |
| + | [[Category: Beta barrel]] | ||
| + | [[Category: Domain-swapped protein]] | ||
| + | [[Category: Fluorescent protein]] | ||
| + | [[Category: Fluorogen activating protein]] | ||
| + | [[Category: Lipocalin]] | ||
Revision as of 11:36, 22 July 2020
Crystal Structure of a Domain-swapped Fluorogen Activating Protein DiB3 Dimer
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