View source for 2wso


==Structure of Cerulean Fluorescent Protein at physiological pH==
<StructureSection load='2wso' size='340' side='right'caption='[[2wso]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WSO 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]] 1.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</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=2wso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wso OCA], [https://pdbe.org/2wso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wso RCSB], [https://www.ebi.ac.uk/pdbsum/2wso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wso ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/2wso_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wso ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enhanced Cyan Fluorescent Protein (ECFP) and its variant Cerulean are genetically-encoded fluorophores widely used as donors in FRET-based cell imaging experiments. First, we have confirmed through denaturation experiments that the double-peak spectroscopic signature of these fluorescent proteins originates from the indole ring of the chromophore. Then, to explain the improvement in the fluorescence properties of Cerulean when compared to ECFP, we have determined the high-resolution crystal structures of these two proteins at physiological pH, and performed molecular dynamics simulations. In both proteins, the N-terminal half of the seventh strand exhibits two conformations that have a complex set of van der Waals interactions with the chromophore and that our simulations suggest interconvert on the nanosecond timescale. The Y145A and H148D mutations in Cerulean stabilize these interactions and allow the chromophore to be more planar, better stabilized and less prone to collisional quenching, albeit only intermittently. As a consequence, the probability of non-radiative decay is significantly decreased. Our results highlight the considerable dynamical flexibility that exists in the vicinity of the tryptophan-based chromophore of these engineered fluorescent proteins, and provide insights which should allow the design of mutants with enhanced optical properties.

Intrinsic dynamics in ECFP and Cerulean control fluorescence quantum yield.,Lelimousin M, Noirclerc-Savoye M, Lazareno-Saez C, Paetzold B, Le Vot S, Chazal R, Macheboeuf P, Field MJ, Bourgeois D, Royant A Biochemistry. 2009 Sep 15. PMID:19754158<ref>PMID:19754158</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wso" style="background-color:#fffaf0;"></div>

==See Also==
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aequorea victoria]]
[[Category: Large Structures]]
[[Category: Bourgeois D]]
[[Category: Chazal R]]
[[Category: Field MJ]]
[[Category: Lazareno-Saez C]]
[[Category: Le Vot S]]
[[Category: Lelimousin M]]
[[Category: Macheboeuf P]]
[[Category: Noirclerc-Savoye M]]
[[Category: Paetzold B]]
[[Category: Royant A]]