View source for 5dtl


==Crystal structure of mEos2-A69T fluorescent protein==
<StructureSection load='5dtl' size='340' side='right'caption='[[5dtl]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dtl]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Lobophyllia_hemprichii Lobophyllia hemprichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DTL 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5SQ:2-[2-[(1~{S})-1-AZANYL-2-(1~{H}-IMIDAZOL-4-YL)ETHYL]-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXIDANYLIDENE-IMIDAZOL-1-YL]ETHANOIC+ACID'>5SQ</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=5dtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dtl OCA], [https://pdbe.org/5dtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dtl RCSB], [https://www.ebi.ac.uk/pdbsum/5dtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dtl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5S6Z9_LOBHE Q5S6Z9_LOBHE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Photoactivated localization microscopy (PALM) is a powerful technique to investigate cellular nanostructures quantitatively and dynamically. However, the use of PALM for molecular counting or single-particle tracking remains limited by the propensity of photoconvertible fluorescent protein markers (PCFPs) to repeatedly enter dark-states. By designing the single-mutants mEos2-A69T and Dendra2-T69A, we completely swapped the blinking behaviors of mEos2 and Dendra2, two popular PCFPs. We combined X-ray crystallography and single-molecule microscopy to show that blinking in mEos2 and Dendra2 is largely controlled by the orientation of arginine 66, a highly-conserved residue in Anthozoan PCFPs. The Arg66 side-chain conformation affects the bleaching and the on-to-off transition quantum yields, as well as the fraction of molecules entering long-lived dark states, resulting in widely different apparent blinking behaviors that largely modulate the efficiency of current blinking correction procedures. The present work provides mechanistic insight into the complex photophysics of Anthozoan PCFPs and will facilitate future engineering of bright and low-blinking variants suitable for PALM microscopy.

Arginine 66 controls dark-state formation in green-to-red photoconvertible fluorescent proteins.,Berardozzi R, Adam V, Martins A, Bourgeois D J Am Chem Soc. 2015 Dec 17. PMID:26675944<ref>PMID:26675944</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dtl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lobophyllia hemprichii]]
[[Category: Adam V]]
[[Category: Berardozzi R]]
[[Category: Bourgeois D]]
[[Category: Martins A]]