5luv: Difference between revisions

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'''Unreleased structure'''


The entry 5luv is ON HOLD  until Paper Publication
==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luv OCA], [http://pdbe.org/5luv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5luv RCSB], [http://www.ebi.ac.uk/pdbsum/5luv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5luv ProSAT]</span></td></tr>
</table>
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5luv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arinkin, V]]
[[Category: Batra-Safferling, R]]
[[Category: Granzin, J]]
[[Category: Apo-state]]
[[Category: Lov domain]]
[[Category: Pas domain]]
[[Category: Signaling protein]]
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