3zuf: Difference between revisions
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< | ==Padron off (non-fluorescent) Btrans== | ||
<StructureSection load='3zuf' size='340' side='right'caption='[[3zuf]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zuf]] is a 6 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=3ZUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZUF 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]] 2.2Å</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=3zuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zuf OCA], [https://pdbe.org/3zuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zuf RCSB], [https://www.ebi.ac.uk/pdbsum/3zuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zuf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5TLG6_9CNID Q5TLG6_9CNID] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Photoactivatable fluorescent proteins are essential players in nanoscopy approaches based on the super-localization of single molecules. The subclass of reversibly photoswitchable fluorescent proteins typically activate through isomerization of the chromophore coupled with a change in its protonation state. However, the interplay between these two events, the details of photoswitching pathways, and the role of protein dynamics remain incompletely understood. Here, by using a combination of structural and spectroscopic approaches, we discovered two fluorescent intermediate states along the on-switching pathway of the fluorescent protein Padron. The first intermediate can be populated at temperatures as low as 100 K and results from a remarkable trans-cis isomerization of the anionic chromophore taking place within a protein matrix essentially deprived of conformational flexibility. This intermediate evolves in the dark at cryotemperatures to a second structurally similar but spectroscopically distinct anionic intermediate. The final fluorescent state, which consists of a mixture of anionic and neutral chromophores in the cis configuration, is only reached above the glass transition temperature, suggesting that chromophore protonation involves solvent interactions mediated by pronounced dynamical breathing of the protein scaffold. The possibility of efficiently and reversibly photoactivating Padron at cryotemperatures will facilitate the development of advanced super-resolution imaging modalities such as cryonanoscopy. | |||
Low-temperature chromophore isomerization reveals the photoswitching mechanism of the fluorescent protein padron.,Regis Faro A, Carpentier P, Jonasson G, Pompidor G, Arcizet D, Demachy I, Bourgeois D J Am Chem Soc. 2011 Oct 19;133(41):16362-5. Epub 2011 Sep 22. PMID:21923132<ref>PMID:21923132</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zuf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dronpa|Dronpa]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Echinophyllia sp. SC22]] | ||
[[ | [[Category: Large Structures]] | ||
[[Category: Bourgeois D]] | |||
== | [[Category: Carpentier P]] | ||
< | [[Category: REGIS Faro A]] | ||
[[Category: Echinophyllia sp. | |||
[[Category: | |||
[[Category: | |||
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Latest revision as of 12:09, 15 November 2023
Padron off (non-fluorescent) BtransPadron off (non-fluorescent) Btrans
Structural highlights
FunctionPublication Abstract from PubMedPhotoactivatable fluorescent proteins are essential players in nanoscopy approaches based on the super-localization of single molecules. The subclass of reversibly photoswitchable fluorescent proteins typically activate through isomerization of the chromophore coupled with a change in its protonation state. However, the interplay between these two events, the details of photoswitching pathways, and the role of protein dynamics remain incompletely understood. Here, by using a combination of structural and spectroscopic approaches, we discovered two fluorescent intermediate states along the on-switching pathway of the fluorescent protein Padron. The first intermediate can be populated at temperatures as low as 100 K and results from a remarkable trans-cis isomerization of the anionic chromophore taking place within a protein matrix essentially deprived of conformational flexibility. This intermediate evolves in the dark at cryotemperatures to a second structurally similar but spectroscopically distinct anionic intermediate. The final fluorescent state, which consists of a mixture of anionic and neutral chromophores in the cis configuration, is only reached above the glass transition temperature, suggesting that chromophore protonation involves solvent interactions mediated by pronounced dynamical breathing of the protein scaffold. The possibility of efficiently and reversibly photoactivating Padron at cryotemperatures will facilitate the development of advanced super-resolution imaging modalities such as cryonanoscopy. Low-temperature chromophore isomerization reveals the photoswitching mechanism of the fluorescent protein padron.,Regis Faro A, Carpentier P, Jonasson G, Pompidor G, Arcizet D, Demachy I, Bourgeois D J Am Chem Soc. 2011 Oct 19;133(41):16362-5. Epub 2011 Sep 22. PMID:21923132[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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