View source for 5luv


==Short LOV protein W619_1 in apo-state==
<StructureSection load='5luv' size='340' side='right'caption='[[5luv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5luv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_W619 Pseudomonas putida W619]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LUV 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]] 2.5&#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=SO4:SULFATE+ION'>SO4</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=5luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luv OCA], [https://pdbe.org/5luv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5luv RCSB], [https://www.ebi.ac.uk/pdbsum/5luv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5luv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B1J385_PSEPW B1J385_PSEPW] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Unique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12-19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 A resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Falpha helix, shortening of the Ealpha-Falpha loop and partial unfolding of the Ealpha helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies.

Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.,Arinkin V, Granzin J, Rollen K, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R Sci Rep. 2017 Feb 17;7:42971. doi: 10.1038/srep42971. PMID:28211532<ref>PMID:28211532</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5luv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida W619]]
[[Category: Arinkin V]]
[[Category: Batra-Safferling R]]
[[Category: Granzin J]]