View source for 5ltq


==Structure of the Yellow Fluorescent Protein lanYFP from Branchiostoma lanceolatum at pH 7.5==
<StructureSection load='5ltq' size='340' side='right'caption='[[5ltq]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ltq]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LTQ 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</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=5ltq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ltq OCA], [https://pdbe.org/5ltq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ltq RCSB], [https://www.ebi.ac.uk/pdbsum/5ltq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ltq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B1PNC0_BRALA B1PNC0_BRALA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for particularly bright oligomeric fluorescent proteins such as the tetrameric yellow fluorescent protein lanYFP from Branchiostoma lanceolatum. A successful monomerization attempt led to the development of the bright yellow-green fluorescent protein mNeonGreen. The structures of lanYFP and mNeonGreen have been determined and compared in order to rationalize the directed evolution process leading from a bright, tetrameric to a still bright, monomeric fluorescent protein. An unusual discolouration of crystals of mNeonGreen was observed after X-ray data collection, which was investigated using a combination of X-ray crystallography and UV-visible absorption and Raman spectroscopies, revealing the effects of specific radiation damage in the chromophore cavity. It is shown that X-rays rapidly lead to the protonation of the phenolate O atom of the chromophore and to the loss of its planarity at the methylene bridge.

Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution.,Clavel D, Gotthard G, von Stetten D, De Sanctis D, Pasquier H, Lambert GG, Shaner NC, Royant A Acta Crystallogr D Struct Biol. 2016 Dec 1;72(Pt 12):1298-1307. Epub 2016 Nov 30. PMID:27917830<ref>PMID:27917830</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ltq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Branchiostoma lanceolatum]]
[[Category: Large Structures]]
[[Category: Clavel D]]
[[Category: Gotthard G]]
[[Category: Royant A]]