5dpg: Difference between revisions
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<StructureSection load='5dpg' size='340' side='right'caption='[[5dpg]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5dpg' size='340' side='right'caption='[[5dpg]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dpg]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5dpg]] 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=5DPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DPG 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]] 1.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CF:4-CYANO-L-PHENYLALANINE'>4CF</scene>, <scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5dpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpg OCA], [https://pdbe.org/5dpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dpg RCSB], [https://www.ebi.ac.uk/pdbsum/5dpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brewer | [[Category: Brewer SH]] | ||
[[Category: Dippel | [[Category: Dippel AB]] | ||
[[Category: Liskov | [[Category: Liskov MT]] | ||
[[Category: Maurici | [[Category: Maurici N]] | ||
[[Category: Olenginski | [[Category: Olenginski GM]] | ||
[[Category: Phillips-Piro | [[Category: Phillips-Piro CM]] | ||
Latest revision as of 00:54, 29 June 2023
sfGFP mutant - 133 p-cyano-L-phenylalaninesfGFP mutant - 133 p-cyano-L-phenylalanine
Structural highlights
FunctionGFP_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. Publication Abstract from PubMedThe X-ray crystal structures of superfolder green fluorescent protein (sfGFP) containing the spectroscopic reporter unnatural amino acids (UAAs) 4-cyano-L-phenylalanine (pCNF) or 4-ethynyl-L-phenylalanine (pCCF) at two unique sites in the protein have been determined. These UAAs were genetically incorporated into sfGFP in a solvent-exposed loop region and/or a partially buried site on the beta-barrel of the protein. The crystal structures containing the UAAs at these two sites permit the structural implications of UAA incorporation for the native protein structure to be assessed with high resolution and permit a direct correlation between the structure and spectroscopic data to be made. The structural implications were quantified by comparing the root-mean-square deviation (r.m.s.d.) between the crystal structure of wild-type sfGFP and the protein constructs containing either pCNF or pCCF in the local environment around the UAAs and in the overall protein structure. The results suggest that the selective placement of these spectroscopic reporter UAAs permits local protein environments to be studied in a relatively nonperturbative fashion with site-specificity. Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study.,Dippel AB, Olenginski GM, Maurici N, Liskov MT, Brewer SH, Phillips-Piro CM Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):121-30. doi:, 10.1107/S2059798315022858. Epub 2016 Jan 1. PMID:26894540[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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