2z6y: Difference between revisions
New page: '''Unreleased structure''' The entry 2z6y is ON HOLD until Paper Publication Authors: Mizuno, H., Kikuchi, A., Ando, R., Jeyakanthan, J., Taka, J., Shiro, Y., Miyawaki, A. Description:... |
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==Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state== | |||
<StructureSection load='2z6y' size='340' side='right'caption='[[2z6y]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2z6y]] 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=2Z6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z6Y 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=2z6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6y OCA], [https://pdbe.org/2z6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z6y RCSB], [https://www.ebi.ac.uk/pdbsum/2z6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z6y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5TLG6_9CNID Q5TLG6_9CNID] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z6/2z6y_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z6y ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structural basis for the photochromism in the fluorescent protein Dronpa is poorly understood, because the crystal structures of the bright state of the protein did not provide an answer to the mechanism of the photochromism, and structural determination of the dark state has been elusive. We performed NMR analyses of Dronpa in solution at ambient temperatures to find structural flexibility of the protein in the dark state. Light-induced changes in interactions between the chromophore and beta-barrel are responsible for switching between the two states. In the bright state, the apex of the chromophore tethers to the barrel by a hydrogen bond, and an imidazole ring protruding from the barrel stabilizes the plane of the chromophore. These interactions are disrupted by strong illumination with blue light, and the chromophore, together with a part of the beta-barrel, becomes flexible, leading to a nonradiative decay process. | |||
Light-dependent regulation of structural flexibility in a photochromic fluorescent protein.,Mizuno H, Mal TK, Walchli M, Kikuchi A, Fukano T, Ando R, Jeyakanthan J, Taka J, Shiro Y, Ikura M, Miyawaki A Proc Natl Acad Sci U S A. 2008 Jul 8;105(27):9227-32. Epub 2008 Jun 23. PMID:18574155<ref>PMID:18574155</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2z6y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dronpa|Dronpa]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Echinophyllia sp. SC22]] | |||
[[Category: Large Structures]] | |||
[[Category: Jeyakanthan J]] | |||
[[Category: Kikuchi A]] | |||
[[Category: Miyawaki A]] | |||
[[Category: Mizuno H]] | |||
[[Category: Shiro Y]] | |||
[[Category: Taka J]] | |||
Latest revision as of 12:39, 6 November 2024
Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-stateCrystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structural basis for the photochromism in the fluorescent protein Dronpa is poorly understood, because the crystal structures of the bright state of the protein did not provide an answer to the mechanism of the photochromism, and structural determination of the dark state has been elusive. We performed NMR analyses of Dronpa in solution at ambient temperatures to find structural flexibility of the protein in the dark state. Light-induced changes in interactions between the chromophore and beta-barrel are responsible for switching between the two states. In the bright state, the apex of the chromophore tethers to the barrel by a hydrogen bond, and an imidazole ring protruding from the barrel stabilizes the plane of the chromophore. These interactions are disrupted by strong illumination with blue light, and the chromophore, together with a part of the beta-barrel, becomes flexible, leading to a nonradiative decay process. Light-dependent regulation of structural flexibility in a photochromic fluorescent protein.,Mizuno H, Mal TK, Walchli M, Kikuchi A, Fukano T, Ando R, Jeyakanthan J, Taka J, Shiro Y, Ikura M, Miyawaki A Proc Natl Acad Sci U S A. 2008 Jul 8;105(27):9227-32. Epub 2008 Jun 23. PMID:18574155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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