5jva: Difference between revisions
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==1.95 angstrom crystal structure of TAGRFP-T== | |||
<StructureSection load='5jva' size='340' side='right' caption='[[5jva]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jva]] is a 4 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t6h 3t6h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JVA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t6h|3t6h]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jva OCA], [http://pdbe.org/5jva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jva RCSB], [http://www.ebi.ac.uk/pdbsum/5jva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jva ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The red fluorescent protein variant TagRFP-T has greatly improved photostability over its parent molecule, TagRFP, but the underlying mechanism leading to this improvement is to date unknown. The 1.95 A resolution crystallographic structure of TagRFP-T showed that its chromophore exists as a mixture of cis and trans coplanar isomers in roughly equal proportions. Interestingly, both isomers are able to fluoresce, a property that has never been observed in any other fluorescent protein. We propose a "circular restoration model" for TagRFP-T to explain its superior photostability: There are four co-existing chromophore states (cis/trans protonated/ionized state) that can be driven by light to transform from one state into another. This model also explains how TagRPF-T essentially eliminates the temporary dark state (reversible photobleaching). | |||
The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability.,Liu R, Liang QN, Du SQ, Hu XJ, Ding Y Biochem Biophys Res Commun. 2016 Aug 19;477(2):229-34. doi:, 10.1016/j.bbrc.2016.06.047. Epub 2016 Jun 11. PMID:27297107<ref>PMID:27297107</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5jva" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hu, X J]] | |||
[[Category: Beta barrel]] | |||
[[Category: Fluorescent protein]] | |||
[[Category: Photostable]] | |||
[[Category: Red fluorescent protein]] | |||
[[Category: Tagrfp-t]] | |||
Revision as of 15:39, 17 May 2017
1.95 angstrom crystal structure of TAGRFP-T
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