This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6ukl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal Structure of a DiB2-split Protein==
==Crystal Structure of a DiB2-split Protein==
-
<StructureSection load='6ukl' size='340' side='right'caption='[[6ukl]]' scene=''>
+
<StructureSection load='6ukl' size='340' side='right'caption='[[6ukl]], [[Resolution|resolution]] 2.02&Aring;' 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=6UKL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UKL FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6ukl]] is a 6 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=6UKL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UKL 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=6ukl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ukl OCA], [http://pdbe.org/6ukl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ukl RCSB], [http://www.ebi.ac.uk/pdbsum/6ukl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ukl 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ukl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ukl OCA], [http://pdbe.org/6ukl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ukl RCSB], [http://www.ebi.ac.uk/pdbsum/6ukl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ukl 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6ukl" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Bacillus coli migula 1895]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Bozhanova NG]]
+
[[Category: Bozhanova, N G]]
-
[[Category: Meiler J]]
+
[[Category: Meiler, J]]
 +
[[Category: Beta barrel]]
 +
[[Category: Fluorescent protein]]
 +
[[Category: Fluorogen activating protein]]
 +
[[Category: Lipocalin]]
 +
[[Category: Split protein]]

Revision as of 11:36, 22 July 2020

Crystal Structure of a DiB2-split Protein

PDB ID 6ukl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools