4p1q
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==GREEN FLUORESCENT PROTEIN E222H VARIANT== | |
| + | <StructureSection load='4p1q' size='340' side='right'caption='[[4p1q]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p1q]] 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=4P1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P1Q 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]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4p1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1q OCA], [https://pdbe.org/4p1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p1q RCSB], [https://www.ebi.ac.uk/pdbsum/4p1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1q 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 == | ||
| + | The widely used green fluorescent protein (GFP) decarboxylates upon irradiation; this involves removal of the acidic function of the glutamic acid at position 222, thereby resulting in the irreversible photoconversion of GFP. To suppress this phenomenon, the photostable, non-photoconvertible histidine was introduced at position 222 in GFP. The variant E222H shows negligible photodynamic processes and high expression yield. In addition, the stable and bright fluorescence over a wide pH range makes the E222H protein an alternative for GFP in fluorescence imaging and spectroscopy. Other fluorescent proteins are predicted to benefit from replacement of the catalytic glutamic acid by histidine. | ||
| - | + | Replacement of Highly Conserved E222 by the Photostable Non-photoconvertible Histidine in GFP.,Auerbach D, Klein M, Franz S, Carius Y, Lancaster CR, Jung G Chembiochem. 2014 Jul 7;15(10):1404-8. doi: 10.1002/cbic.201402075. Epub 2014 Jun, 11. PMID:24919579<ref>PMID:24919579</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4p1q" 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: Auerbach D]] | ||
| + | [[Category: Carius Y]] | ||
| + | [[Category: Franz S]] | ||
| + | [[Category: Jung G]] | ||
| + | [[Category: Klein M]] | ||
| + | [[Category: Lancaster CRD]] | ||
Current revision
GREEN FLUORESCENT PROTEIN E222H VARIANT
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