View source for 4ohs


==The structure of a far-red fluorescent protein, AQ143==
<StructureSection load='4ohs' size='340' side='right'caption='[[4ohs]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ohs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinia_equina Actinia equina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OHS 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]] 2.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CH6:{(4Z)-2-[(1S)-1-AMINO-3-(METHYLSULFANYL)PROPYL]-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CH6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ohs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ohs OCA], [https://pdbe.org/4ohs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ohs RCSB], [https://www.ebi.ac.uk/pdbsum/4ohs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ohs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2VFP3_ACTEQ Q2VFP3_ACTEQ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineering fluorescent proteins (FPs) to emit light at longer wavelengths is a significant focus in the development of the next generation of fluorescent biomarkers, as far-red light penetrates tissue with minimal absorption, allowing better imaging inside of biological hosts. Structure-guided design and directed evolution have led to the discovery of red FPs with significant bathochromic shifts to their emission. Here, we present the crystal structure of one of the most bathochromically shifted FPs reported to date, AQ143, a nine-point mutant of aeCP597, a chromoprotein from Actinia equina. The 2.19 A resolution structure reveals several important chromophore interactions that contribute to the protein's far-red emission and shows dual occupancy of the green and red chromophores.

The structure of a far-red fluorescent protein, AQ143, shows evidence in support of reported red-shifting chromophore interactions.,Wannier TM, Mayo SL Protein Sci. 2014 Jun 3. doi: 10.1002/pro.2498. PMID:24888769<ref>PMID:24888769</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ohs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Actinia equina]]
[[Category: Large Structures]]
[[Category: Mayo SL]]
[[Category: Wannier TM]]