2ye1: Difference between revisions

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'''Unreleased structure'''


The entry 2ye1 is ON HOLD
==X-ray structure of the cyan fluorescent proteinmTurquoise-GL (K206A mutant)==
<StructureSection load='2ye1' size='340' side='right'caption='[[2ye1]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ye1]] 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=2YE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YE1 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]] 1.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SWG:2-[(4Z)-2-[(1R)-1-AMINO-2-HYDROXY-ETHYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-IMIDAZOL-1-YL]ETHANOIC+ACID'>SWG</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=2ye1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ye1 OCA], [https://pdbe.org/2ye1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ye1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ye1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ye1 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Optimization of autofluorescent proteins by intensity-based screening of bacteria does not necessarily identify the brightest variant for eukaryotes. We report a strategy to screen excited state lifetimes, which identified cyan fluorescent proteins with long fluorescence lifetimes (&gt;3.7 ns) and high quantum yields (&gt;0.8). One variant, mTurquoise, was 1.5-fold brighter than mCerulean in mammalian cells and decayed mono-exponentially, making it an excellent fluorescence resonance energy transfer (FRET) donor.


Authors: von Stetten, D., Goedhart, J., Noirclerc-Savoye, M., Lelimousin, M., Joosen, L., Hink, M.A., van Weeren, L., Gadella, T.W.J., Royant, A.
Bright cyan fluorescent protein variants identified by fluorescence lifetime screening.,Goedhart J, van Weeren L, Hink MA, Vischer NO, Jalink K, Gadella TW Jr Nat Methods. 2010 Feb;7(2):137-9. Epub 2010 Jan 17. PMID:020081836<ref>PMID:020081836</ref>


Description: X-ray structure of the cyan fluorescent protein Turquoise-GL
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ye1" 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: Gadella TWJ]]
[[Category: Goedhart J]]
[[Category: Noirclerc-Savoye M]]
[[Category: Royant A]]
[[Category: Von Stetten D]]

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