View source for 7mfy


==The Crystal Structure of Q108K:K40L:T51V:T53S:R58W:Y19W:A33W:L117E Mutant of HCRBPII Bound with LizFluor==
<StructureSection load='7mfy' size='340' side='right'caption='[[7mfy]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MFY 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]] 1.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZFG:4-{5-[(2E)-but-2-en-2-yl]thiophen-2-yl}-N,N-dimethylaniline'>ZFG</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=7mfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mfy OCA], [https://pdbe.org/7mfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mfy RCSB], [https://www.ebi.ac.uk/pdbsum/7mfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mfy ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The incredible potential for fluorescent proteins to revolutionize biology has inspired the development of a variety of design strategies to address an equally broad range of photophysical characteristics, depending on potential applications. Of these, fluorescent proteins that simultaneously exhibit high quantum yield, red-shifted emission, and wide separation between excitation and emission wavelengths (Large Stokes Shift, LSS) are rare. The pursuit of LSS systems has led to the formation of a complex, obtained from the marriage of a rationally engineered protein (human cellular retinol binding protein II, hCRBPII) and different fluorogenic molecules, capable of supporting photobase activity. The large increase in basicity upon photoexcitation leads to protonation of the fluorophore in the excited state, dramatically red-shifting its emission, leading to an LSS protein/fluorophore complex. Essential for selective photobase activity is the intimate involvement of the target protein structure and sequence that enables Excited State Proton Transfer (ESPT). The potential power and usefulness of the strategy was demonstrated in live cell imaging of human cell lines.

Design of Large Stokes Shift Fluorescent Proteins Based on Excited State Proton Transfer of an Engineered Photobase.,Santos EM, Sheng W, Esmatpour Salmani R, Tahmasebi Nick S, Ghanbarpour A, Gholami H, Vasileiou C, Geiger JH, Borhan B J Am Chem Soc. 2021 Sep 22;143(37):15091-15102. doi: 10.1021/jacs.1c05039. Epub, 2021 Sep 13. PMID:34516091<ref>PMID:34516091</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mfy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Geiger J]]
[[Category: Ghanbarpour A]]