6nqj: Difference between revisions
New page: '''Unreleased structure''' The entry 6nqj is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)== | |||
<StructureSection load='6nqj' size='340' side='right'caption='[[6nqj]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nqj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Echinophyllia_sp._SC22 Echinophyllia sp. SC22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NQJ 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GYC:[(4Z)-2-[(1R)-1-AMINO-2-MERCAPTOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYC</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=6nqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqj OCA], [https://pdbe.org/6nqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nqj RCSB], [https://www.ebi.ac.uk/pdbsum/6nqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5TLG6_9CNID Q5TLG6_9CNID] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. | |||
Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714<ref>PMID:31896714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6nqj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dronpa|Dronpa]] | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Echinophyllia sp. SC22]] | |||
[[Category: Large Structures]] | |||
[[Category: Boxer SG]] | |||
[[Category: Lin C-Y]] | |||
[[Category: Mathews II]] | |||
[[Category: Romei MG]] | |||
Latest revision as of 09:58, 11 October 2023
Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)
Structural highlights
FunctionPublication Abstract from PubMedRotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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