2ye1: Difference between revisions
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<StructureSection load='2ye1' size='340' side='right'caption='[[2ye1]], [[Resolution|resolution]] 1.63Å' scene=''> | <StructureSection load='2ye1' size='340' side='right'caption='[[2ye1]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ye1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63Å</td></tr> | ||
<tr id=' | <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> | <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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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 (>3.7 ns) and high quantum yields (>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. | 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 (>3.7 ns) and high quantum yields (>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. | ||
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: | 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> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gadella | [[Category: Gadella TWJ]] | ||
[[Category: Goedhart | [[Category: Goedhart J]] | ||
[[Category: Noirclerc-Savoye | [[Category: Noirclerc-Savoye M]] | ||
[[Category: Royant | [[Category: Royant A]] | ||
[[Category: Stetten | [[Category: Von Stetten D]] | ||
Latest revision as of 08:06, 23 October 2024
X-ray structure of the cyan fluorescent proteinmTurquoise-GL (K206A mutant)
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