View source for 4edo


==Crystal structure of far-red fluorescent protein eqFP650==
<StructureSection load='4edo' size='340' side='right'caption='[[4edo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4edo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entacmaea_quadricolor Entacmaea quadricolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</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=4edo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edo OCA], [https://pdbe.org/4edo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edo RCSB], [https://www.ebi.ac.uk/pdbsum/4edo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edo ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/J9PBR7_ENTQU J9PBR7_ENTQU]] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the far-red fluorescent proteins (FPs) eqFP650 (lambda(ex)(max)/lambda(em)(max) 592/650 nm) and eqFP670 (lambda(ex)(max)/lambda(em)(max) 605/670 nm), the successors of the far-red FP Katushka (lambda(ex)(max)/lambda(em)(max) 588/635 nm), have been determined at 1.8 and 1.6 A resolution, respectively. An examination of the structures demonstrated that there are two groups of changes responsible for the bathochromic shift of excitation/emission bands of these proteins relative to their predecessor. The first group of changes resulted in an increase of hydrophilicity at the acylimine site of the chromophore due to the presence of one and three water molecules in eqFP650 and eqFP670, respectively. These water molecules provide connection of the chromophore with the protein scaffold via hydrogen bonds causing an ~15 nm bathochromic shift of the eqFP650 and eqFP670 emission bands. The second group of changes observed in eqFP670 arises from substitution of both Ser143 and Ser158 by asparagines. Asn143 and Asn158 of eqFP670 are hydrogen bonded with each other, as well as with the protein scaffold and with the p-hydroxyphenyl group of the chromophore, resulting in an additional ~20 nm bathochromic shift of the eqFP670 emission band as compared to eqFP650. The role of the observed structural changes was verified by mutagenesis.

Structural basis for bathochromic shift of fluorescence in far-red fluorescent proteins eqFP650 and eqFP670.,Pletnev S, Pletneva NV, Souslova EA, Chudakov DM, Lukyanov S, Wlodawer A, Dauter Z, Pletnev V Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1088-97. doi:, 10.1107/S0907444912020598. Epub 2012 Aug 18. PMID:22948909<ref>PMID:22948909</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4edo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Entacmaea quadricolor]]
[[Category: Large Structures]]
[[Category: Pletnev S]]
[[Category: Pletnev VZ]]
[[Category: Pletneva NV]]