5wj2: Difference between revisions
New page: '''Unreleased structure''' The entry 5wj2 is ON HOLD until Paper Publication Authors: Liu, C., Campbell, B.C., Petsko, G.A. Description: Crystal structure of the green fluorescent prot... |
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==Crystal structure of the green fluorescent protein Clover== | |||
<StructureSection load='5wj2' size='340' side='right'caption='[[5wj2]], [[Resolution|resolution]] 2.41Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5wj2]] is a 2 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=5WJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WJ2 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]] 2.409Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</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=5wj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj2 OCA], [https://pdbe.org/5wj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wj2 RCSB], [https://www.ebi.ac.uk/pdbsum/5wj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj2 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 == | |||
We have determined the crystal structure of Clover, one of the brightest fluorescent proteins, and found that its T203H/S65G mutations relative to wild-type GFP lock the critical E222 side chain in a fixed configuration that mimics the major conformer of that in EGFP. The resulting equilibrium shift to the predominantly deprotonated chromophore increases the extinction coefficient (EC), opposes photoactivation, and is responsible for the bathochromic shift. Clover's brightness can further be attributed to a pi-pi stacking interaction between H203 and the chromophore. Consistent with these observations, the Clover G65S mutant reversed the equilibrium shift, dramatically decreased the EC, and made Clover photoactivatable under conditions that activated photoactivatable GFP. Using the Clover structure, we rationally engineered a non-photoactivatable redox sensor, roClover1, and determined its structure as well as that of its parental template, roClover0.1. These high-resolution structures provide deeper insights into structure-function relationships in GFPs and may aid the development of excitation-improved ratiometric biosensors. | |||
Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors.,Campbell BC, Petsko GA, Liu CF Structure. 2017 Dec 27. pii: S0969-2126(17)30405-7. doi:, 10.1016/j.str.2017.12.006. PMID:29307487<ref>PMID:29307487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Campbell | <div class="pdbe-citations 5wj2" style="background-color:#fffaf0;"></div> | ||
[[Category: Liu | |||
[[Category: Petsko | ==See Also== | ||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aequorea victoria]] | |||
[[Category: Large Structures]] | |||
[[Category: Campbell BC]] | |||
[[Category: Liu C]] | |||
[[Category: Petsko GA]] | |||
Latest revision as of 17:14, 4 October 2023
Crystal structure of the green fluorescent protein CloverCrystal structure of the green fluorescent protein Clover
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 PubMedWe have determined the crystal structure of Clover, one of the brightest fluorescent proteins, and found that its T203H/S65G mutations relative to wild-type GFP lock the critical E222 side chain in a fixed configuration that mimics the major conformer of that in EGFP. The resulting equilibrium shift to the predominantly deprotonated chromophore increases the extinction coefficient (EC), opposes photoactivation, and is responsible for the bathochromic shift. Clover's brightness can further be attributed to a pi-pi stacking interaction between H203 and the chromophore. Consistent with these observations, the Clover G65S mutant reversed the equilibrium shift, dramatically decreased the EC, and made Clover photoactivatable under conditions that activated photoactivatable GFP. Using the Clover structure, we rationally engineered a non-photoactivatable redox sensor, roClover1, and determined its structure as well as that of its parental template, roClover0.1. These high-resolution structures provide deeper insights into structure-function relationships in GFPs and may aid the development of excitation-improved ratiometric biosensors. Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors.,Campbell BC, Petsko GA, Liu CF Structure. 2017 Dec 27. pii: S0969-2126(17)30405-7. doi:, 10.1016/j.str.2017.12.006. PMID:29307487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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